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6wsl

Cryo-EM structure of VASH1-SVBP bound to microtubules

Method: ELECTRON MICROSCOPY Dmax: 149.3 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Tubulin alpha-1A chain

Homo sapiens

UniProt Q71U36

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric（8） Consistent with protein copy count Chain A； UniProt 1–451 Chain E； UniProt 1–451 Not recorded Tubulin beta-3 chain × 2 （Q13509） Tubulinyl-Tyr carboxypeptidase 1 × 2 （Q7L8A9） Small vasohibin-binding protein × 2 （Q8N300） GTP GUANOSINE-5'-TRIPHOSPHATE × 2 G2P PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER × 2 ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.10 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB Difference from Current Entry 6WSL Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
22AJ GDP human alpha1A/beta3 S239C microtubule Deposited 2026-01-05 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–451（451 aa）
Not recorded MG MAGNESIUM ION × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 1 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 6.8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.48 Å
22AK GDP human alpha1A/beta3 microtubule Deposited 2026-01-05 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–451（451 aa）
Not recorded GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 2 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 6.8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.41 Å
5JCO Structure and dynamics of single-isoform recombinant neuronal human tubulin Deposited 2016-04-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain A 1–437（437 aa）
Chain B 1–437（437 aa）
Chain E 1–437（437 aa）
Chain F 1–437（437 aa）
Chain G 1–437（437 aa）
Chain H 1–437（437 aa）
Not recorded G2P PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER × 6 MG MAGNESIUM ION × 12 GTP GUANOSINE-5'-TRIPHOSPHATE × 6 ELECTRON MICROSCOPY
cryo-EM buffer pH 6.9
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.00 Å
7UN1 8-nm repeat of the human sperm tip singlet microtubule Deposited 2022-04-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 109 PDB declaration: 109-meric
Chain AC 1–451（451 aa）
Chain AE 1–451（451 aa）
Chain BC 1–451（451 aa）
Chain BE 1–451（451 aa）
Chain BG 1–451（451 aa）
Chain CC 1–451（451 aa）
Chain CE 1–451（451 aa）
Chain CG 1–451（451 aa）
Chain DC 1–451（451 aa）
Chain DE 1–451（451 aa）
Chain DG 1–451（451 aa）
Chain EC 1–451（451 aa）
Chain EE 1–451（451 aa）
Chain EG 1–451（451 aa）
Chain FC 1–451（451 aa）
Chain FE 1–451（451 aa）
Chain FG 1–451（451 aa）
Chain GC 1–451（451 aa）
Chain GE 1–451（451 aa）
Chain GG 1–451（451 aa）
Chain HC 1–451（451 aa）
Chain HE 1–451（451 aa）
Chain HG 1–451（451 aa）
Chain IC 1–451（451 aa）
Chain IE 1–451（451 aa）
Chain IG 1–451（451 aa）
Chain JC 1–451（451 aa）
Chain JE 1–451（451 aa）
Chain JG 1–451（451 aa）
Chain KC 1–451（451 aa）
Chain KE 1–451（451 aa）
Chain KG 1–451（451 aa）
Chain LA 1–451（451 aa）
Chain LC 1–451（451 aa）
Chain LE 1–451（451 aa）
Chain MA 1–451（451 aa）
Chain MC 1–451（451 aa）
Chain ME 1–451（451 aa）
Not recorded GDP GUANOSINE-5'-DIPHOSPHATE × 38 GTP GUANOSINE-5'-TRIPHOSPHATE × 38 MG MAGNESIUM ION × 38 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 6.00 Å
7UNG 48-nm repeat of the human respiratory doublet microtubule Deposited 2022-04-11 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 435 PDB declaration: 435-meric
Chain AA 1–451（451 aa）
Chain AC 1–451（451 aa）
Chain AE 1–451（451 aa）
Chain AG 1–451（451 aa）
Chain AI 1–451（451 aa）
Chain AK 1–451（451 aa）
Chain AM 1–451（451 aa）
Chain BA 1–451（451 aa）
Chain BC 1–451（451 aa）
Chain BE 1–451（451 aa）
Chain BG 1–451（451 aa）
Chain BI 1–451（451 aa）
Chain BK 1–451（451 aa）
Chain BM 1–451（451 aa）
Chain CA 1–451（451 aa）
Chain CC 1–451（451 aa）
Chain CE 1–451（451 aa）
Chain CG 1–451（451 aa）
Chain CI 1–451（451 aa）
Chain CK 1–451（451 aa）
Chain CM 1–451（451 aa）
Chain DA 1–451（451 aa）
Chain DC 1–451（451 aa）
Chain DE 1–451（451 aa）
Chain DG 1–451（451 aa）
Chain DI 1–451（451 aa）
Chain DK 1–451（451 aa）
Chain DM 1–451（451 aa）
Chain EC 1–451（451 aa）
Chain EE 1–451（451 aa）
Chain EG 1–451（451 aa）
Chain EI 1–451（451 aa）
Chain EK 1–451（451 aa）
Chain EM 1–451（451 aa）
Chain FC 1–451（451 aa）
Chain FE 1–451（451 aa）
Chain FG 1–451（451 aa）
Chain FI 1–451（451 aa）
Chain FK 1–451（451 aa）
Chain FM 1–451（451 aa）
Chain GC 1–451（451 aa）
Chain GE 1–451（451 aa）
Chain GG 1–451（451 aa）
Chain GI 1–451（451 aa）
Chain GK 1–451（451 aa）
Chain GM 1–451（451 aa）
Chain HC 1–451（451 aa）
Chain HE 1–451（451 aa）
Chain HG 1–451（451 aa）
Chain HI 1–451（451 aa）
Chain HK 1–451（451 aa）
Chain HM 1–451（451 aa）
Chain HO 1–451（451 aa）
Chain IC 1–451（451 aa）
Chain IE 1–451（451 aa）
Chain IG 1–451（451 aa）
Chain II 1–451（451 aa）
Chain IK 1–451（451 aa）
Chain IM 1–451（451 aa）
Chain IO 1–451（451 aa）
Chain JC 1–451（451 aa）
Chain JE 1–451（451 aa）
Chain JG 1–451（451 aa）
Chain JI 1–451（451 aa）
Chain JK 1–451（451 aa）
Chain JM 1–451（451 aa）
Chain KC 1–451（451 aa）
Chain KE 1–451（451 aa）
Chain KG 1–451（451 aa）
Chain KI 1–451（451 aa）
Chain KK 1–451（451 aa）
Chain KM 1–451（451 aa）
Chain KO 1–451（451 aa）
Chain LC 1–451（451 aa）
Chain LE 1–451（451 aa）
Chain LG 1–451（451 aa）
Chain LI 1–451（451 aa）
Chain LK 1–451（451 aa）
Chain LM 1–451（451 aa）
Chain MC 1–451（451 aa）
Chain ME 1–451（451 aa）
Chain MG 1–451（451 aa）
Chain MI 1–451（451 aa）
Chain MK 1–451（451 aa）
Chain MM 1–451（451 aa）
Chain NC 1–451（451 aa）
Chain NE 1–451（451 aa）
Chain NG 1–451（451 aa）
Chain NI 1–451（451 aa）
Chain NK 1–451（451 aa）
Chain NM 1–451（451 aa）
Chain OC 1–451（451 aa）
Chain OE 1–451（451 aa）
Chain OG 1–451（451 aa）
Chain OI 1–451（451 aa）
Chain OK 1–451（451 aa）
Chain OM 1–451（451 aa）
Chain OO 1–451（451 aa）
Chain PC 1–451（451 aa）
Chain PE 1–451（451 aa）
Chain PG 1–451（451 aa）
Chain PI 1–451（451 aa）
Chain PK 1–451（451 aa）
Chain PM 1–451（451 aa）
Chain PO 1–451（451 aa）
Chain QC 1–451（451 aa）
Chain QE 1–451（451 aa）
Chain QG 1–451（451 aa）
Chain QI 1–451（451 aa）
Chain QK 1–451（451 aa）
Chain QM 1–451（451 aa）
Chain QO 1–451（451 aa）
Chain RC 1–451（451 aa）
Chain RE 1–451（451 aa）
Chain RG 1–451（451 aa）
Chain RI 1–451（451 aa）
Chain RK 1–451（451 aa）
Chain RM 1–451（451 aa）
Chain RO 1–451（451 aa）
Chain SE 1–451（451 aa）
Chain SG 1–451（451 aa）
Chain SI 1–451（451 aa）
Chain SK 1–451（451 aa）
Chain SM 1–451（451 aa）
Chain SO 1–451（451 aa）
Chain TE 1–451（451 aa）
Chain TG 1–451（451 aa）
Chain TI 1–451（451 aa）
Chain TK 1–451（451 aa）
Chain TM 1–451（451 aa）
Chain TO 1–451（451 aa）
Chain UE 1–451（451 aa）
Chain UG 1–451（451 aa）
Chain UI 1–451（451 aa）
Chain UK 1–451（451 aa）
Chain UM 1–451（451 aa）
Chain UO 1–451（451 aa）
Chain VE 1–451（451 aa）
Chain VG 1–451（451 aa）
Chain VI 1–451（451 aa）
Chain VK 1–451（451 aa）
Chain VM 1–451（451 aa）
Chain VO 1–451（451 aa）
Chain WE 1–451（451 aa）
Chain WG 1–451（451 aa）
Chain WI 1–451（451 aa）
Chain WK 1–451（451 aa）
Chain WM 1–451（451 aa）
Chain WO 1–451（451 aa）
Not recorded GTP GUANOSINE-5'-TRIPHOSPHATE × 149 MG MAGNESIUM ION × 149 GDP GUANOSINE-5'-DIPHOSPHATE × 153 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.3
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.60 Å
8J07 96nm repeat of human respiratory doublet microtubule and associated axonemal complexes Deposited 2023-04-09 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 974 PDB declaration: 974-meric
Chain AC 1–451（451 aa）
Chain AE 1–451（451 aa）
Chain AG 1–451（451 aa）
Chain AI 1–451（451 aa）
Chain AK 1–451（451 aa）
Chain AM 1–451（451 aa）
Chain AO 1–451（451 aa）
Chain AQ 1–451（451 aa）
Chain AS 1–451（451 aa）
Chain AU 1–451（451 aa）
Chain AW 1–451（451 aa）
Chain AY 1–451（451 aa）
Chain AZ 1–451（451 aa）
Chain BA 1–451（451 aa）
Chain BC 1–451（451 aa）
Chain BE 1–451（451 aa）
Chain BG 1–451（451 aa）
Chain BI 1–451（451 aa）
Chain BK 1–451（451 aa）
Chain BM 1–451（451 aa）
Chain BO 1–451（451 aa）
Chain BQ 1–451（451 aa）
Chain BS 1–451（451 aa）
Chain BU 1–451（451 aa）
Chain BW 1–451（451 aa）
Chain BY 1–451（451 aa）
Chain CC 1–451（451 aa）
Chain CE 1–451（451 aa）
Chain CG 1–451（451 aa）
Chain CI 1–451（451 aa）
Chain CK 1–451（451 aa）
Chain CM 1–451（451 aa）
Chain CO 1–451（451 aa）
Chain CQ 1–451（451 aa）
Chain CS 1–451（451 aa）
Chain CU 1–451（451 aa）
Chain CW 1–451（451 aa）
Chain CY 1–451（451 aa）
Chain DC 1–451（451 aa）
Chain DE 1–451（451 aa）
Chain DG 1–451（451 aa）
Chain DI 1–451（451 aa）
Chain DK 1–451（451 aa）
Chain DM 1–451（451 aa）
Chain DO 1–451（451 aa）
Chain DQ 1–451（451 aa）
Chain DS 1–451（451 aa）
Chain DU 1–451（451 aa）
Chain DW 1–451（451 aa）
Chain DY 1–451（451 aa）
Chain EC 1–451（451 aa）
Chain EE 1–451（451 aa）
Chain EG 1–451（451 aa）
Chain EI 1–451（451 aa）
Chain EK 1–451（451 aa）
Chain EM 1–451（451 aa）
Chain EO 1–451（451 aa）
Chain EQ 1–451（451 aa）
Chain ES 1–451（451 aa）
Chain EU 1–451（451 aa）
Chain EW 1–451（451 aa）
Chain EY 1–451（451 aa）
Chain FC 1–451（451 aa）
Chain FE 1–451（451 aa）
Chain FG 1–451（451 aa）
Chain FI 1–451（451 aa）
Chain FK 1–451（451 aa）
Chain FM 1–451（451 aa）
Chain FO 1–451（451 aa）
Chain FQ 1–451（451 aa）
Chain FS 1–451（451 aa）
Chain FU 1–451（451 aa）
Chain FW 1–451（451 aa）
Chain FY 1–451（451 aa）
Chain GC 1–451（451 aa）
Chain GE 1–451（451 aa）
Chain GG 1–451（451 aa）
Chain GI 1–451（451 aa）
Chain GK 1–451（451 aa）
Chain GM 1–451（451 aa）
Chain GO 1–451（451 aa）
Chain GQ 1–451（451 aa）
Chain GS 1–451（451 aa）
Chain GU 1–451（451 aa）
Chain GW 1–451（451 aa）
Chain GY 1–451（451 aa）
Chain HA 1–451（451 aa）
Chain HC 1–451（451 aa）
Chain HE 1–451（451 aa）
Chain HG 1–451（451 aa）
Chain HI 1–451（451 aa）
Chain HK 1–451（451 aa）
Chain HM 1–451（451 aa）
Chain HO 1–451（451 aa）
Chain HQ 1–451（451 aa）
Chain HS 1–451（451 aa）
Chain HU 1–451（451 aa）
Chain HW 1–451（451 aa）
Chain HY 1–451（451 aa）
Chain IA 1–451（451 aa）
Chain IC 1–451（451 aa）
Chain IE 1–451（451 aa）
Chain IG 1–451（451 aa）
Chain II 1–451（451 aa）
Chain IK 1–451（451 aa）
Chain IM 1–451（451 aa）
Chain IO 1–451（451 aa）
Chain IQ 1–451（451 aa）
Chain IS 1–451（451 aa）
Chain IU 1–451（451 aa）
Chain IW 1–451（451 aa）
Chain IY 1–451（451 aa）
Chain JC 1–451（451 aa）
Chain JE 1–451（451 aa）
Chain JG 1–451（451 aa）
Chain JI 1–451（451 aa）
Chain JK 1–451（451 aa）
Chain JM 1–451（451 aa）
Chain JO 1–451（451 aa）
Chain JQ 1–451（451 aa）
Chain JS 1–451（451 aa）
Chain JU 1–451（451 aa）
Chain JW 1–451（451 aa）
Chain JY 1–451（451 aa）
Chain KC 1–451（451 aa）
Chain KE 1–451（451 aa）
Chain KG 1–451（451 aa）
Chain KI 1–451（451 aa）
Chain KK 1–451（451 aa）
Chain KM 1–451（451 aa）
Chain KO 1–451（451 aa）
Chain KQ 1–451（451 aa）
Chain KS 1–451（451 aa）
Chain KU 1–451（451 aa）
Chain KW 1–451（451 aa）
Chain KY 1–451（451 aa）
Chain LC 1–451（451 aa）
Chain LE 1–451（451 aa）
Chain LG 1–451（451 aa）
Chain LI 1–451（451 aa）
Chain LK 1–451（451 aa）
Chain LM 1–451（451 aa）
Chain LO 1–451（451 aa）
Chain LQ 1–451（451 aa）
Chain LS 1–451（451 aa）
Chain LU 1–451（451 aa）
Chain LW 1–451（451 aa）
Chain LY 1–451（451 aa）
Chain MA 1–451（451 aa）
Chain MC 1–451（451 aa）
Chain ME 1–451（451 aa）
Chain MG 1–451（451 aa）
Chain MI 1–451（451 aa）
Chain MK 1–451（451 aa）
Chain MM 1–451（451 aa）
Chain MO 1–451（451 aa）
Chain MQ 1–451（451 aa）
Chain MS 1–451（451 aa）
Chain MU 1–451（451 aa）
Chain MW 1–451（451 aa）
Chain MY 1–451（451 aa）
Chain NA 1–451（451 aa）
Chain NC 1–451（451 aa）
Chain NE 1–451（451 aa）
Chain NG 1–451（451 aa）
Chain NI 1–451（451 aa）
Chain NK 1–451（451 aa）
Chain NM 1–451（451 aa）
Chain NO 1–451（451 aa）
Chain NQ 1–451（451 aa）
Chain NS 1–451（451 aa）
Chain NU 1–451（451 aa）
Chain NW 1–451（451 aa）
Chain OA 1–451（451 aa）
Chain OC 1–451（451 aa）
Chain OE 1–451（451 aa）
Chain OG 1–451（451 aa）
Chain OI 1–451（451 aa）
Chain OK 1–451（451 aa）
Chain OM 1–451（451 aa）
Chain OO 1–451（451 aa）
Chain OQ 1–451（451 aa）
Chain OS 1–451（451 aa）
Chain OU 1–451（451 aa）
Chain OW 1–451（451 aa）
Chain OY 1–451（451 aa）
Chain PA 1–451（451 aa）
Chain PC 1–451（451 aa）
Chain PE 1–451（451 aa）
Chain PG 1–451（451 aa）
Chain PI 1–451（451 aa）
Chain PK 1–451（451 aa）
Chain PM 1–451（451 aa）
Chain PO 1–451（451 aa）
Chain PQ 1–451（451 aa）
Chain PS 1–451（451 aa）
Chain PU 1–451（451 aa）
Chain PW 1–451（451 aa）
Chain PY 1–451（451 aa）
Chain QA 1–451（451 aa）
Chain QC 1–451（451 aa）
Chain QE 1–451（451 aa）
Chain QG 1–451（451 aa）
Chain QI 1–451（451 aa）
Chain QK 1–451（451 aa）
Chain QM 1–451（451 aa）
Chain QO 1–451（451 aa）
Chain QQ 1–451（451 aa）
Chain QS 1–451（451 aa）
Chain QU 1–451（451 aa）
Chain QW 1–451（451 aa）
Chain QY 1–451（451 aa）
Chain RA 1–451（451 aa）
Chain RC 1–451（451 aa）
Chain RE 1–451（451 aa）
Chain RG 1–451（451 aa）
Chain RI 1–451（451 aa）
Chain RK 1–451（451 aa）
Chain RM 1–451（451 aa）
Chain RO 1–451（451 aa）
Chain RQ 1–451（451 aa）
Chain RS 1–451（451 aa）
Chain RU 1–451（451 aa）
Chain RW 1–451（451 aa）
Chain RY 1–451（451 aa）
Chain SC 1–451（451 aa）
Chain SE 1–451（451 aa）
Chain SG 1–451（451 aa）
Chain SI 1–451（451 aa）
Chain SK 1–451（451 aa）
Chain SM 1–451（451 aa）
Chain SO 1–451（451 aa）
Chain SQ 1–451（451 aa）
Chain SS 1–451（451 aa）
Chain SU 1–451（451 aa）
Chain SW 1–451（451 aa）
Chain SY 1–451（451 aa）
Chain TC 1–451（451 aa）
Chain TE 1–451（451 aa）
Chain TG 1–451（451 aa）
Chain TI 1–451（451 aa）
Chain TK 1–451（451 aa）
Chain TM 1–451（451 aa）
Chain TO 1–451（451 aa）
Chain TQ 1–451（451 aa）
Chain TS 1–451（451 aa）
Chain TU 1–451（451 aa）
Chain TW 1–451（451 aa）
Chain TY 1–451（451 aa）
Chain UC 1–451（451 aa）
Chain UE 1–451（451 aa）
Chain UG 1–451（451 aa）
Chain UI 1–451（451 aa）
Chain UK 1–451（451 aa）
Chain UM 1–451（451 aa）
Chain UO 1–451（451 aa）
Chain UQ 1–451（451 aa）
Chain US 1–451（451 aa）
Chain UU 1–451（451 aa）
Chain UW 1–451（451 aa）
Chain UY 1–451（451 aa）
Chain VC 1–451（451 aa）
Chain VE 1–451（451 aa）
Chain VG 1–451（451 aa）
Chain VI 1–451（451 aa）
Chain VK 1–451（451 aa）
Chain VM 1–451（451 aa）
Chain VO 1–451（451 aa）
Chain VQ 1–451（451 aa）
Chain VS 1–451（451 aa）
Chain VU 1–451（451 aa）
Chain VW 1–451（451 aa）
Chain VY 1–451（451 aa）
Chain WA 1–451（451 aa）
Chain WC 1–451（451 aa）
Chain WE 1–451（451 aa）
Chain WG 1–451（451 aa）
Chain WI 1–451（451 aa）
Chain WK 1–451（451 aa）
Chain WM 1–451（451 aa）
Chain WO 1–451（451 aa）
Chain WQ 1–451（451 aa）
Chain WS 1–451（451 aa）
Chain WU 1–451（451 aa）
Chain WW 1–451（451 aa）
Not recorded GTP GUANOSINE-5'-TRIPHOSPHATE × 285 MG MAGNESIUM ION × 285 GDP GUANOSINE-5'-DIPHOSPHATE × 289 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.3
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.10 Å
8SH7 TUBB4B and TUBA1A Heterodimer from Human Respiratory Doublet Microtubules Deposited 2023-04-13 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–451（451 aa）
Not recorded GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.3
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.80 Å
9OX7 In situ microtubule structure in the axon of a human neuron Deposited 2025-06-03 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain A 1–451（451 aa）
Chain C 1–451（451 aa）
Chain G 1–451（451 aa）
Chain H 1–451（451 aa）
Not recorded GDP GUANOSINE-5'-DIPHOSPHATE × 4 MG MAGNESIUM ION × 4 GTP GUANOSINE-5'-TRIPHOSPHATE × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.2
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.69 Å
9WD7 GMPCPP-stabilizsd human alpha1A/beta3 microtubule Deposited 2025-08-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain a 1–451（451 aa）
Not recorded GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 2 G2P PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 6.8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.34 Å
9WD9 GMPCPP-stabilized human alpha1A/beta3 S239C microtubule Deposited 2025-08-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain a 1–451（451 aa）
Not recorded GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 2 G2P PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 6.8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.26 Å
9WDA Paclitaxel/GMPCPP-stabilized human alpha1A/beta3 microtubule Deposited 2025-08-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain a 1–451（451 aa）
Not recorded MG MAGNESIUM ION × 2 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 TA1 TAXOL × 1 G2P PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 6.8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.35 Å
9WDB Paclitaxel/GMPCPP-stabilized human alpha1A/beta3 S239C microtubule Deposited 2025-08-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain a 1–451（451 aa）
Not recorded GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 2 TA1 TAXOL × 1 G2P PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 6.8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.39 Å

12 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TBA1A_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–451； UniProt 1–451 Author chain E； PDBConstruct 1–451； UniProt 1–451

Tubulin beta-3 chain

Homo sapiens

UniProt Q13509

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric（8） Consistent with protein copy count Chain B； UniProt 1–450 Chain F； UniProt 1–450 Not recorded Tubulin alpha-1A chain × 2 （Q71U36） Tubulinyl-Tyr carboxypeptidase 1 × 2 （Q7L8A9） Small vasohibin-binding protein × 2 （Q8N300） GTP GUANOSINE-5'-TRIPHOSPHATE × 2 G2P PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER × 2 ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.10 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB Difference from Current Entry 6WSL Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
22AJ GDP human alpha1A/beta3 S239C microtubule Deposited 2026-01-05 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–450（450 aa）
Mutation：S239C MG MAGNESIUM ION × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 1 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 6.8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.48 Å
22AK GDP human alpha1A/beta3 microtubule Deposited 2026-01-05 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–450（450 aa）
Not recorded GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 2 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 6.8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.41 Å
5IJ0 Cryo EM density of microtubule assembled from human TUBB3 Deposited 2016-03-01 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–426（426 aa）
Not recorded GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 6.9
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.80 Å
5IJ9 Cryo EM density of microtubule assembled from human TUBB3-D417H mutant Deposited 2016-03-01 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–426（426 aa）
Mutation：D417H GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 6.9
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.70 Å
5JCO Structure and dynamics of single-isoform recombinant neuronal human tubulin Deposited 2016-04-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain C 1–426（426 aa）
Chain D 1–426（426 aa）
Chain I 1–426（426 aa）
Chain J 1–426（426 aa）
Chain K 1–426（426 aa）
Chain L 1–426（426 aa）
Not recorded G2P PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER × 6 MG MAGNESIUM ION × 12 GTP GUANOSINE-5'-TRIPHOSPHATE × 6 ELECTRON MICROSCOPY
cryo-EM buffer pH 6.9
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.00 Å
6E7B 13-pf 3-start GMPCPP-human alpha1B/beta3 microtubules Deposited 2018-07-25 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–426（426 aa）
Not recorded MG MAGNESIUM ION × 2 G2P PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER × 1 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 6.8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.50 Å
6S8L Structure, Thermodynamics, and Kinetics of Plinabulin Binding to two Tubulin Isotypes Deposited 2019-07-10 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain B 1–450（450 aa）
Not recorded GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 2 PN6 (3Z,6Z)-3-benzylidene-6-[(5-tert-butyl-1H-imidazol-4-yl)methylidene]piperazine-2,5-dione × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；293 K；100 mM Bis-TrisMethane, pH 5.5, supplemented with 200 mM ammonium sulfate and 25% PEG3350
Resolution 1.80 Å R-free 0.266
7LXB HeLa-tubulin in complex with cryptophycin 52 Deposited 2021-03-03 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric
Chain B 1–450（450 aa）
Chain D 1–450（450 aa）
Chain F 1–450（450 aa）
Chain H 1–450（450 aa）
Chain J 1–450（450 aa）
Chain L 1–450（450 aa）
Chain N 1–450（450 aa）
Chain P 1–450（450 aa）
Not recorded GTP GUANOSINE-5'-TRIPHOSPHATE × 8 YGY Cryptophycin 52 × 8 GDP GUANOSINE-5'-DIPHOSPHATE × 8 ELECTRON MICROSCOPY
cryo-EM buffer pH 6.9
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.26 Å
7M18 HeLa-tubulin in complex with cryptophycin 1 Deposited 2021-03-12 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric
Chain B 1–450（450 aa）
Chain D 1–450（450 aa）
Chain F 1–450（450 aa）
Chain H 1–450（450 aa）
Chain J 1–450（450 aa）
Chain L 1–450（450 aa）
Chain N 1–450（450 aa）
Chain P 1–450（450 aa）
Not recorded YNP Cryptophycin 1 × 8 GDP GUANOSINE-5'-DIPHOSPHATE × 8 GTP GUANOSINE-5'-TRIPHOSPHATE × 8 ELECTRON MICROSCOPY
cryo-EM buffer pH 6.9
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.38 Å
7M20 18-mer HeLa-tubulin rings in complex with Cryptophycin 1 Deposited 2021-03-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 18 PDB declaration: octadecameric
Chain B 1–450（450 aa）
Chain D 1–450（450 aa）
Chain F 1–450（450 aa）
Chain H 1–450（450 aa）
Chain J 1–450（450 aa）
Chain L 1–450（450 aa）
Chain N 1–450（450 aa）
Chain P 1–450（450 aa）
Chain R 1–450（450 aa）
Not recorded GDP GUANOSINE-5'-DIPHOSPHATE × 9 YNP Cryptophycin 1 × 9 GTP GUANOSINE-5'-TRIPHOSPHATE × 9 ELECTRON MICROSCOPY
cryo-EM buffer pH 6.9
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.84 Å
7PJF Inhibiting parasite proliferation using a rationally designed anti-tubulin agent Deposited 2021-08-24 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain B 1–450（450 aa）
Not recorded GTP GUANOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 5.5；293 K；100 mM Bis-TrisMethane, pH 5.5, supplemented with 200 mM ammonium sulfate and 25% PEG3350
Resolution 1.86 Å R-free 0.218
7SJ7 Undecorated 13pf wildtype microtubule from recombinant human tubulin Deposited 2021-10-16 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain B 1–450（450 aa）
Chain D 1–450（450 aa）
Chain F 1–450（450 aa）
Chain G 1–450（450 aa）
Chain H 1–450（450 aa）
Chain I 1–450（450 aa）
Not recorded GTP GUANOSINE-5'-TRIPHOSPHATE × 6 MG MAGNESIUM ION × 6 GDP GUANOSINE-5'-DIPHOSPHATE × 6 ELECTRON MICROSCOPY
cryo-EM buffer pH 6.8；80 mM PIPES, 1 mM EGTA, 5 mM MgCl2, 2 mM GTP, pH 6.8
cryo-EM vitrification conditions Cryogen ETHANE-PROPANE
Resolution 3.80 Å
7SJ8 13pf wildtype microtubule from recombinant human tubulin decorated with kinesin Deposited 2021-10-16 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain B 1–450（450 aa）
Chain D 1–450（450 aa）
Chain F 1–450（450 aa）
Chain G 1–450（450 aa）
Chain H 1–450（450 aa）
Chain I 1–450（450 aa）
Not recorded GTP GUANOSINE-5'-TRIPHOSPHATE × 6 MG MAGNESIUM ION × 6 GDP GUANOSINE-5'-DIPHOSPHATE × 6 ELECTRON MICROSCOPY
cryo-EM buffer pH 6.8；80 mM PIPES, 1 mM EGTA, 5 mM MgCl2, 2 mM GTP, pH 6.8
cryo-EM vitrification conditions Cryogen ETHANE-PROPANE；30 second adsorption time onto grid. blot force 15, 4 second blot time, 37 degrees, and 100 percent humidity. 0.5 second drain time.
Resolution 3.60 Å
7SJ9 13pf E254A microtubule from recombinant human tubulin decorated with EB3 Deposited 2021-10-16 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 14 PDB declaration: tetradecameric
Chain B 1–450（450 aa）
Chain D 1–450（450 aa）
Chain F 1–450（450 aa）
Chain G 1–450（450 aa）
Chain H 1–450（450 aa）
Chain I 1–450（450 aa）
Not recorded GTP GUANOSINE-5'-TRIPHOSPHATE × 12 MG MAGNESIUM ION × 12 ELECTRON MICROSCOPY
cryo-EM buffer pH 6.8；80 mM PIPES, 1 mM EGTA, 5 mM MgCl2, 2 mM GTP, pH 6.8
cryo-EM vitrification conditions Cryogen ETHANE-PROPANE
Resolution 3.80 Å
7SJA Undecorated 13pf E254N microtubule from recombinant human tubulin Deposited 2021-10-16 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain B 1–450（450 aa）
Chain D 1–450（450 aa）
Chain F 1–450（450 aa）
Chain G 1–450（450 aa）
Chain H 1–450（450 aa）
Chain I 1–450（450 aa）
Not recorded GTP GUANOSINE-5'-TRIPHOSPHATE × 12 MG MAGNESIUM ION × 12 ELECTRON MICROSCOPY
cryo-EM buffer pH 6.8；80 mM PIPES, 1 mM EGTA, 5 mM MgCl2, 2 mM GTP, pH 6.8
cryo-EM vitrification conditions Cryogen ETHANE-PROPANE
Resolution 3.80 Å
7Z6S MATCAP bound to a human 14 protofilament microtubule Deposited 2022-03-14 Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: Hexameric
Chain B 1–450（450 aa）
Chain H 1–450（450 aa）
Not recorded GTP GUANOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 2 ZN ZINC ION × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 6.9
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.90 Å
8VRJ Rigid body fitted model for gamma tubulin ring complex capped microtubule Deposited 2024-01-22 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 60 PDB declaration: 60-meric
Chain 2 1–450（450 aa）
Chain o 1–450（450 aa）
Chain p 1–450（450 aa）
Chain q 1–450（450 aa）
Chain r 1–450（450 aa）
Chain s 1–450（450 aa）
Chain t 1–450（450 aa）
Chain u 1–450（450 aa）
Chain v 1–450（450 aa）
Chain w 1–450（450 aa）
Chain x 1–450（450 aa）
Chain y 1–450（450 aa）
Chain z 1–450（450 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 6.8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 7.70 Å
8VRK Rigid body fitted model for refined density map of gamma tubulin ring complex capped microtubule Deposited 2024-01-22 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 60 PDB declaration: 60-meric
Chain 2 1–450（450 aa）
Chain o 1–450（450 aa）
Chain p 1–450（450 aa）
Chain q 1–450（450 aa）
Chain r 1–450（450 aa）
Chain s 1–450（450 aa）
Chain t 1–450（450 aa）
Chain u 1–450（450 aa）
Chain v 1–450（450 aa）
Chain w 1–450（450 aa）
Chain x 1–450（450 aa）
Chain y 1–450（450 aa）
Chain z 1–450（450 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 6.8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 8.50 Å
8VT7 Structure of the gamma tubulin ring complex nucleated microtubule protofilament. Deposited 2024-01-25 Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 1–450（450 aa）
Chain F 1–450（450 aa）
Not recorded GDP GUANOSINE-5'-DIPHOSPHATE × 2 GTP GUANOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 6.8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.66 Å
9F3B Undecorated 13pf E254Q microtubule from recombinant human tubulin Deposited 2024-04-25 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: 12-meric
Chain B 1–450（450 aa）
Chain D 1–450（450 aa）
Chain F 1–450（450 aa）
Chain N 1–450（450 aa）
Chain P 1–450（450 aa）
Chain R 1–450（450 aa）
Not recorded GTP GUANOSINE-5'-TRIPHOSPHATE × 12 MG MAGNESIUM ION × 12 ELECTRON MICROSCOPY
cryo-EM buffer pH 6.8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.60 Å
9F3H Undecorated 13pf mosaic 20%E254Q - 80% E254QN microtubule from recombinant human tubulin Deposited 2024-04-25 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: 12-meric
Chain B 1–450（450 aa）
Chain D 1–450（450 aa）
Chain F 1–450（450 aa）
Chain N 1–450（450 aa）
Chain P 1–450（450 aa）
Chain R 1–450（450 aa）
Not recorded GTP GUANOSINE-5'-TRIPHOSPHATE × 12 MG MAGNESIUM ION × 12 ELECTRON MICROSCOPY
cryo-EM buffer pH 6.8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.30 Å
9F3R 13pf E254Q microtubule from recombinant human tubulin decorated with EB3 Deposited 2024-04-25 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 14 PDB declaration: 14-meric
Chain B 1–450（450 aa）
Chain D 1–450（450 aa）
Chain F 1–450（450 aa）
Chain N 1–450（450 aa）
Chain P 1–450（450 aa）
Chain R 1–450（450 aa）
Not recorded GTP GUANOSINE-5'-TRIPHOSPHATE × 12 MG MAGNESIUM ION × 12 ELECTRON MICROSCOPY
cryo-EM buffer pH 6.8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.30 Å
9F3S 13pf mosaic 20%E254Q - 80% E254N microtubule from recombinant human tubulin decorated with EB3 Deposited 2024-04-25 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 14 PDB declaration: 14-meric
Chain B 1–450（450 aa）
Chain D 1–450（450 aa）
Chain F 1–450（450 aa）
Chain N 1–450（450 aa）
Chain P 1–450（450 aa）
Chain R 1–450（450 aa）
Not recorded GTP GUANOSINE-5'-TRIPHOSPHATE × 12 MG MAGNESIUM ION × 12 ELECTRON MICROSCOPY
cryo-EM buffer pH 6.8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.20 Å
9SMX CM1-activated gTuRC in complex with nascent alpha-E254D mutant microtubules Deposited 2025-09-09 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 73 PDB declaration: 73-meric
Chain BB 1–450（450 aa）
Chain CB 1–450（450 aa）
Chain DB 1–450（450 aa）
Chain EB 1–450（450 aa）
Chain FB 1–450（450 aa）
Chain GB 1–450（450 aa）
Chain HB 1–450（450 aa）
Chain IB 1–450（450 aa）
Chain JB 1–450（450 aa）
Chain KB 1–450（450 aa）
Chain LB 1–450（450 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) GTP GUANOSINE-5'-TRIPHOSPHATE × 11 ELECTRON MICROSCOPY
cryo-EM buffer pH 6.9
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.67 Å
9WD7 GMPCPP-stabilizsd human alpha1A/beta3 microtubule Deposited 2025-08-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain b 1–450（450 aa）
Not recorded GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 2 G2P PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 6.8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.34 Å
9WD9 GMPCPP-stabilized human alpha1A/beta3 S239C microtubule Deposited 2025-08-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain b 1–450（450 aa）
Mutation：S239C GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 2 G2P PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 6.8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.26 Å
9WDA Paclitaxel/GMPCPP-stabilized human alpha1A/beta3 microtubule Deposited 2025-08-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain b 1–450（450 aa）
Not recorded MG MAGNESIUM ION × 2 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 TA1 TAXOL × 1 G2P PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 6.8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.35 Å
9WDB Paclitaxel/GMPCPP-stabilized human alpha1A/beta3 S239C microtubule Deposited 2025-08-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain b 1–450（450 aa）
Mutation：S239c GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 2 TA1 TAXOL × 1 G2P PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 6.8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.39 Å

28 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TBB3_HUMAN
Isoform —
PDB entities 2
Chains and sequence ranges Author chain B； PDBConstruct 1–450； UniProt 1–450 Author chain F； PDBConstruct 1–450； UniProt 1–450

Tubulinyl-Tyr carboxypeptidase 1

Homo sapiens

UniProt Q7L8A9

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric（8） Consistent with protein copy count Chain C； UniProt 52–310 Chain G； UniProt 52–310 Not recorded Tubulin alpha-1A chain × 2 （Q71U36） Tubulin beta-3 chain × 2 （Q13509） Small vasohibin-binding protein × 2 （Q8N300） GTP GUANOSINE-5'-TRIPHOSPHATE × 2 G2P PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER × 2 ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.10 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB Difference from Current Entry 6WSL Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
6J4U Structural basis of tubulin detyrosination by vasohibins-SVBP enzyme complex and functional implications Deposited 2019-01-10 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 57–307（251 aa）
Mutation：E71S/A72H/K79M No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；pH 5；293 K；by introducing three mutations E71S/A72H/K79M into V1c allowed us to solve the V1c-SVBP to high resolution. Well diffracting crystals of the mutant V1c-SVBP complex were obtained in 1.0 M lithium chloride, 0.1 M citric acid, pH 5.0, 20% PEG 6000.
Resolution 2.00 Å R-free 0.204
6J7B Crystal structure of VASH1-SVBP in complex with epoY Deposited 2019-01-17 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 57–306（250 aa）
Not recorded BJL N-[(3R)-4-ethoxy-3-hydroxy-4-oxobutanoyl]-L-tyrosine × 1 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；pH 6；293 K；20%PEG6000, 1M lithium chloride, 0.1M MES pH6.0
Resolution 1.62 Å R-free 0.197
6J8F Crystal structure of SVBP-VASH1 with peptide mimic the C-terminal of alpha-tubulin Deposited 2019-01-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain B 70–306（237 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；0.1M Na citrate tribasic dihydrate pH 5.0, 18% PEG 20000
Resolution 2.28 Å R-free 0.237
6J8N Crystal structure of SVBP-VASH1 complex, mutation C169A of VASH1 Deposited 2019-01-20 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 70–306（237 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；6% v/v Tacsimate pH6.0, 0.1M MES monohydrate pH 6.0, 25% PEG 4000
Resolution 1.95 Å R-free 0.210
6J8N Crystal structure of SVBP-VASH1 complex, mutation C169A of VASH1 Deposited 2019-01-20 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain D 70–306（237 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；6% v/v Tacsimate pH6.0, 0.1M MES monohydrate pH 6.0, 25% PEG 4000
Resolution 1.95 Å R-free 0.210
6J8O Structure of a hypothetical protease Deposited 2019-01-20 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain B 70–306（237 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；0.1M BIS-TRIS pH 6.5, 16% polyethylene glycol 10000
Resolution 1.85 Å R-free 0.195
6J91 Structure of a hypothetical protease Deposited 2019-01-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 70–306（237 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；0.1M Na citrate tribasic dihydrate pH 5.5, 16% PEG 8000, 0.01M Cadmium chloride hydrate
Resolution 3.50 Å R-free 0.258
6J9H Crystal structure of SVBP-VASH1 complex Deposited 2019-01-22 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 70–306（237 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；0.1M Na citrate tribasic dihydrate pH 5.5, 16% PEG 8000, 0.01M Cadmium chloride hydrate
Resolution 2.31 Å R-free 0.271
6J9H Crystal structure of SVBP-VASH1 complex Deposited 2019-01-22 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain D 70–306（237 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；0.1M Na citrate tribasic dihydrate pH 5.5, 16% PEG 8000, 0.01M Cadmium chloride hydrate
Resolution 2.31 Å R-free 0.271
6K81 Crystal structure of human VASH1-SVBP complex Deposited 2019-06-11 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–365（365 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；293 K；Calcium acetate, PEG 3000
Resolution 2.28 Å R-free 0.242
6LPG human VASH1-SVBP complex Deposited 2020-01-10 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 56–310（255 aa）
Not recorded SO4 SULFATE ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.16 M ammonium sulfate, 0.08 M Sodium acetate pH4.6, 20%(w/v) PEG4000, 20%(v/v) glycerol
Resolution 2.30 Å R-free 0.236
6NVQ Crystal structure of the VASH1-SVBP complex Deposited 2019-02-05 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 1–315（315 aa）
Mutation：C169A GOL GLYCEROL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.8；293 K；19% PEG 3000, 0.1M Tris-HCl, 0.2M calcium chloride
Resolution 2.10 Å R-free 0.214
6OCF The crystal structure of VASH1-SVBP complex Deposited 2019-03-23 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 58–305（248 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) GOL GLYCEROL × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；293.15 K；0.1 M sodium citrate tribasic dihydrate, pH 5.0, and 18% (w/v) PEG20000
Resolution 2.10 Å R-free 0.222
6OCG Crystal structure of VASH1-SVBP complex bound with EpoY Deposited 2019-03-23 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 59–305（247 aa）
Not recorded CL CHLORIDE ION × 1 GOL GLYCEROL × 1 BJL N-[(3R)-4-ethoxy-3-hydroxy-4-oxobutanoyl]-L-tyrosine × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；293.15 K；5% (v/v) TacsimateTM, 0.1 M HEPES, pH 7.0, and 10% (w/v) polyethylene glycol monomethyl ether 5,000
Resolution 1.83 Å R-free 0.219
6OCH Crystal structure of VASH1-SVBP complex bound with parthenolide Deposited 2019-03-23 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 61–302（242 aa）
Not recorded M4Y parthenolide × 1 GOL GLYCEROL × 1 SO4 SULFATE ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293.15 K；0.2 M ammonium sulfate, 0.1 M Bis-tris, pH 5.5, and 25 % (w/v) PEG 3350
Resolution 2.00 Å R-free 0.229
6OCH Crystal structure of VASH1-SVBP complex bound with parthenolide Deposited 2019-03-23 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 61–302（242 aa）
Not recorded M4Y parthenolide × 1 SO4 SULFATE ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293.15 K；0.2 M ammonium sulfate, 0.1 M Bis-tris, pH 5.5, and 25 % (w/v) PEG 3350
Resolution 2.00 Å R-free 0.229

13 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VASH1_HUMAN
Isoform —
PDB entities 3
Chains and sequence ranges Author chain C； PDBConstruct 1–259； UniProt 52–310 Author chain G； PDBConstruct 1–259； UniProt 52–310

Small vasohibin-binding protein

Homo sapiens

UniProt Q8N300

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric（8） Consistent with protein copy count Chain D； UniProt 1–66 Chain H； UniProt 1–66 Not recorded Tubulin alpha-1A chain × 2 （Q71U36） Tubulin beta-3 chain × 2 （Q13509） Tubulinyl-Tyr carboxypeptidase 1 × 2 （Q7L8A9） GTP GUANOSINE-5'-TRIPHOSPHATE × 2 G2P PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER × 2 ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.10 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB Difference from Current Entry 6WSL Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
6J4O Structural basis of tubulin detyrosination by vasohibins-SVBP enzyme complex and functional implications Deposited 2019-01-10 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–66（66 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) GOL GLYCEROL × 5 PO4 PHOSPHATE ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；pH 8.2；293 K；1.6 M sodium/potassium phosphate, pH 8.2
Resolution 2.30 Å R-free 0.224
6J4P Structural basis of tubulin detyrosination by vasohibins-SVBP enzyme complex and functional implications Deposited 2019-01-10 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–66（66 aa）
Not recorded BJL N-[(3R)-4-ethoxy-3-hydroxy-4-oxobutanoyl]-L-tyrosine × 1 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；pH 7；293 K；V2c-SVBP was mixed with the inhibitor epoY at a mole ratio of 1:5 and incubated on ice for 30 min. Then, the resulting co-complex of V2c-SVBP-epoY was crystallized in 1.0 M lithium chloride, 0.1 M HEPES, pH 7.0, 20% PEG 6000.
Resolution 1.60 Å R-free 0.188
6J4Q Structural basis of tubulin detyrosination by vasohibins-SVBP enzyme complex and functional implications Deposited 2019-01-10 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–66（66 aa）
Not recorded TQ8 N-[(2S)-4-chloro-3-oxo-1-phenyl-butan-2-yl]-4-methyl-benzenesulfonamide × 2 GOL GLYCEROL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；pH 7；293 K；V2c-SVBP was mixed with the inhibitor TPCK at a mole ratio of 1:5 and incubated on ice for 30 min. Then, the resulting co-complex of V2c-SVBP-TPCK was crystallized in 1.0 M sodium malonate, pH 7.0.
Resolution 2.70 Å R-free 0.247
6J4Q Structural basis of tubulin detyrosination by vasohibins-SVBP enzyme complex and functional implications Deposited 2019-01-10 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain D 1–66（66 aa）
Not recorded TQ8 N-[(2S)-4-chloro-3-oxo-1-phenyl-butan-2-yl]-4-methyl-benzenesulfonamide × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；pH 7；293 K；V2c-SVBP was mixed with the inhibitor TPCK at a mole ratio of 1:5 and incubated on ice for 30 min. Then, the resulting co-complex of V2c-SVBP-TPCK was crystallized in 1.0 M sodium malonate, pH 7.0.
Resolution 2.70 Å R-free 0.247
6J4Q Structural basis of tubulin detyrosination by vasohibins-SVBP enzyme complex and functional implications Deposited 2019-01-10 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain G 1–66（66 aa）
Not recorded TQ8 N-[(2S)-4-chloro-3-oxo-1-phenyl-butan-2-yl]-4-methyl-benzenesulfonamide × 2 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；pH 7；293 K；V2c-SVBP was mixed with the inhibitor TPCK at a mole ratio of 1:5 and incubated on ice for 30 min. Then, the resulting co-complex of V2c-SVBP-TPCK was crystallized in 1.0 M sodium malonate, pH 7.0.
Resolution 2.70 Å R-free 0.247
6J4Q Structural basis of tubulin detyrosination by vasohibins-SVBP enzyme complex and functional implications Deposited 2019-01-10 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain K 1–66（66 aa）
Not recorded TQ8 N-[(2S)-4-chloro-3-oxo-1-phenyl-butan-2-yl]-4-methyl-benzenesulfonamide × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；pH 7；293 K；V2c-SVBP was mixed with the inhibitor TPCK at a mole ratio of 1:5 and incubated on ice for 30 min. Then, the resulting co-complex of V2c-SVBP-TPCK was crystallized in 1.0 M sodium malonate, pH 7.0.
Resolution 2.70 Å R-free 0.247
6J4S Structural basis of tubulin detyrosination by vasohibins-SVBP enzyme complex and functional implications Deposited 2019-01-10 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–66（66 aa）
Not recorded GOL GLYCEROL × 3 PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；pH 6.8；293 K；full-length V2-SVBP complex at a concentration of 15 mg/mL was crystallized in 1.8 M sodium/potassium phosphate, pH 6.8
Resolution 2.80 Å R-free 0.227
6J4U Structural basis of tubulin detyrosination by vasohibins-SVBP enzyme complex and functional implications Deposited 2019-01-10 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–66（66 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；pH 5；293 K；by introducing three mutations E71S/A72H/K79M into V1c allowed us to solve the V1c-SVBP to high resolution. Well diffracting crystals of the mutant V1c-SVBP complex were obtained in 1.0 M lithium chloride, 0.1 M citric acid, pH 5.0, 20% PEG 6000.
Resolution 2.00 Å R-free 0.204
6J4V Structural basis of tubulin detyrosination by vasohibins-SVBP enzyme complex and functional implications Deposited 2019-01-10 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain B 1–66（66 aa）
Mutation：C58S PO4 PHOSPHATE ION × 2 GOL GLYCEROL × 4 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；pH 8.2；293 K；For crystallization of V2c-SVBP C58S in complex with the maTail peptide the components were mixed in a 1:3 molar ratio and incubated at room temperature for 24 h before setting up crystallization trials. The resulting V2c-SVBP S58C-maTail complex was crystallized in 1.4 M sodium/potassium phosphate, pH 8.2.
Resolution 2.10 Å R-free 0.200
6J7B Crystal structure of VASH1-SVBP in complex with epoY Deposited 2019-01-17 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–52（52 aa）
Not recorded BJL N-[(3R)-4-ethoxy-3-hydroxy-4-oxobutanoyl]-L-tyrosine × 1 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；pH 6；293 K；20%PEG6000, 1M lithium chloride, 0.1M MES pH6.0
Resolution 1.62 Å R-free 0.197
6J8F Crystal structure of SVBP-VASH1 with peptide mimic the C-terminal of alpha-tubulin Deposited 2019-01-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain A 3–48（46 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；0.1M Na citrate tribasic dihydrate pH 5.0, 18% PEG 20000
Resolution 2.28 Å R-free 0.237
6J8N Crystal structure of SVBP-VASH1 complex, mutation C169A of VASH1 Deposited 2019-01-20 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–66（66 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；6% v/v Tacsimate pH6.0, 0.1M MES monohydrate pH 6.0, 25% PEG 4000
Resolution 1.95 Å R-free 0.210
6J8N Crystal structure of SVBP-VASH1 complex, mutation C169A of VASH1 Deposited 2019-01-20 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 1–66（66 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；6% v/v Tacsimate pH6.0, 0.1M MES monohydrate pH 6.0, 25% PEG 4000
Resolution 1.95 Å R-free 0.210
6J8O Structure of a hypothetical protease Deposited 2019-01-20 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain A 3–49（47 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；0.1M BIS-TRIS pH 6.5, 16% polyethylene glycol 10000
Resolution 1.85 Å R-free 0.195
6J91 Structure of a hypothetical protease Deposited 2019-01-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–66（66 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；0.1M Na citrate tribasic dihydrate pH 5.5, 16% PEG 8000, 0.01M Cadmium chloride hydrate
Resolution 3.50 Å R-free 0.258
6J9H Crystal structure of SVBP-VASH1 complex Deposited 2019-01-22 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–66（66 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；0.1M Na citrate tribasic dihydrate pH 5.5, 16% PEG 8000, 0.01M Cadmium chloride hydrate
Resolution 2.31 Å R-free 0.271
6J9H Crystal structure of SVBP-VASH1 complex Deposited 2019-01-22 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 1–66（66 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；0.1M Na citrate tribasic dihydrate pH 5.5, 16% PEG 8000, 0.01M Cadmium chloride hydrate
Resolution 2.31 Å R-free 0.271
6JZC Structural basis of tubulin detyrosination Deposited 2019-05-01 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain D 1–66（66 aa）
Not recorded GOL GLYCEROL × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；291.15 K；HEPES, Ammonium sulphate, potassium chloride
Resolution 2.20 Å R-free 0.215
6JZC Structural basis of tubulin detyrosination Deposited 2019-05-01 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 1–66（66 aa）
Not recorded GOL GLYCEROL × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；291.15 K；HEPES, Ammonium sulphate, potassium chloride
Resolution 2.20 Å R-free 0.215
6JZD Crystal structure of peptide-bound VASH2-SVBP complex Deposited 2019-05-01 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain B 1–66（66 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；291.15 K；HEPES, potassium chloride, Ammonium sulphate
Resolution 2.48 Å R-free 0.230
6JZE Crystal structure of VASH2-SVBP complex with the magic triangle I3C Deposited 2019-05-01 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–66（66 aa）
Not recorded I3C 5-amino-2,4,6-triiodobenzene-1,3-dicarboxylic acid × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291.15 K；BIS-TRIS propane, Sodium formate
Resolution 2.51 Å R-free 0.266
6K81 Crystal structure of human VASH1-SVBP complex Deposited 2019-06-11 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–66（66 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；293 K；Calcium acetate, PEG 3000
Resolution 2.28 Å R-free 0.242
6LPG human VASH1-SVBP complex Deposited 2020-01-10 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 2–66（65 aa）
Not recorded SO4 SULFATE ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.16 M ammonium sulfate, 0.08 M Sodium acetate pH4.6, 20%(w/v) PEG4000, 20%(v/v) glycerol
Resolution 2.30 Å R-free 0.236
6NVQ Crystal structure of the VASH1-SVBP complex Deposited 2019-02-05 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–66（66 aa）
Not recorded GOL GLYCEROL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.8；293 K；19% PEG 3000, 0.1M Tris-HCl, 0.2M calcium chloride
Resolution 2.10 Å R-free 0.214
6OCF The crystal structure of VASH1-SVBP complex Deposited 2019-03-23 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 18–66（49 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) GOL GLYCEROL × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；293.15 K；0.1 M sodium citrate tribasic dihydrate, pH 5.0, and 18% (w/v) PEG20000
Resolution 2.10 Å R-free 0.222
6OCG Crystal structure of VASH1-SVBP complex bound with EpoY Deposited 2019-03-23 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 26–51（26 aa）
Not recorded CL CHLORIDE ION × 1 GOL GLYCEROL × 1 BJL N-[(3R)-4-ethoxy-3-hydroxy-4-oxobutanoyl]-L-tyrosine × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；293.15 K；5% (v/v) TacsimateTM, 0.1 M HEPES, pH 7.0, and 10% (w/v) polyethylene glycol monomethyl ether 5,000
Resolution 1.83 Å R-free 0.219
6OCH Crystal structure of VASH1-SVBP complex bound with parthenolide Deposited 2019-03-23 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 25–52（28 aa）
Not recorded M4Y parthenolide × 1 GOL GLYCEROL × 1 SO4 SULFATE ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293.15 K；0.2 M ammonium sulfate, 0.1 M Bis-tris, pH 5.5, and 25 % (w/v) PEG 3350
Resolution 2.00 Å R-free 0.229
6OCH Crystal structure of VASH1-SVBP complex bound with parthenolide Deposited 2019-03-23 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain D 25–52（28 aa）
Not recorded M4Y parthenolide × 1 SO4 SULFATE ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293.15 K；0.2 M ammonium sulfate, 0.1 M Bis-tris, pH 5.5, and 25 % (w/v) PEG 3350
Resolution 2.00 Å R-free 0.229
6QBY Crystal structure of VASH 2 in complex with SVBP Deposited 2018-12-24 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–66（66 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293.15 K；0.2M Sodium formate 0.1M Bis-Tris propane pH 6.5 20% PEG3350
Resolution 2.09 Å R-free 0.230
6QBY Crystal structure of VASH 2 in complex with SVBP Deposited 2018-12-24 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain D 1–66（66 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293.15 K；0.2M Sodium formate 0.1M Bis-Tris propane pH 6.5 20% PEG3350
Resolution 2.09 Å R-free 0.230
7ZCW Cryo-EM structure of GMPCPP-microtubules in complex with VASH2-SVBP Deposited 2022-03-29 Different construct Different mutation/modification Different ligand/ion Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain D 1–66（66 aa）
Not recorded GTP GUANOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 6 G2P PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.60 Å

23 other PDB entries and 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SVBP_HUMAN
Isoform —
PDB entities 4
Chains and sequence ranges Author chain D； PDBConstruct 1–66； UniProt 1–66 Author chain H； PDBConstruct 1–66； UniProt 1–66

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 6wsl

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6wsl
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6wsl
Deposition date deposition_date2020-05-01
Structure title titleCryo-EM structure of VASH1-SVBP bound to microtubules
Keywords keywordsMicrotubule, Posttranslational modification, Detyrosination, Vasohibin, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodELECTRON MICROSCOPY
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier44.86 Å
Radius of gyration Rg (electron density) rg_electron44.56 Å
Forward intensity I(0) i01013800000.00
Molecular weight molecular_weight259130.0 kDa
Excluded volume excluded_volume322370 ų
Envelope volume envelope_volume434540 ų
Hydration-shell volume shell_volume79731 ų
Envelope diameter envelope_diameter156.5 Å
Shell Rg shell_rg50.39 Å
Envelope Rg envelope_rg44.35 Å
Shape Rg shape_rg44.59 Å
Total Rg total_rg44.74 Å
Total atoms total_atoms18204
Residues n_residues2278
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax149.3 Å
Rg (real space) rg_real44.83 Å
Rg uncertainty (real space) rg_real_error1.31 Å
I(0) (real space) i0_real1.0140e+09
I(0) uncertainty (real space) i0_real_error1.9120e+07
Rg (reciprocal space) rg_reciprocal44.86 Å
I(0) (reciprocal space) i0_reciprocal1014000000.0000
Solution quality estimate total_estimate0.8647
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary59.7 Å
Skewness Skewness skewness0.362
Kurtosis Kurtosis kurtosis-0.141
Angular range angular_range— – 0.1750 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha210700000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.836; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.731
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (6)

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7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (8 domains)

Domain ID domain_idd6wsla1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.32 — Tubulin nucleotide-binding domain-like
Superfamily Superfamily superfamilyc.32.1 — Tubulin nucleotide-binding domain-like
Family Family familyc.32.1.1 — Tubulin, GTPase domain
Domain ID domain_idd6wsla2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.79 — Bacillus chorismate mutase-like
Superfamily Superfamily superfamilyd.79.2 — Tubulin C-terminal domain-like
Family Family familyd.79.2.1 — Tubulin, C-terminal domain
Domain ID domain_idd6wslb1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.32 — Tubulin nucleotide-binding domain-like
Superfamily Superfamily superfamilyc.32.1 — Tubulin nucleotide-binding domain-like
Family Family familyc.32.1.1 — Tubulin, GTPase domain
Domain ID domain_idd6wslb2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.79 — Bacillus chorismate mutase-like
Superfamily Superfamily superfamilyd.79.2 — Tubulin C-terminal domain-like
Family Family familyd.79.2.1 — Tubulin, C-terminal domain
Domain ID domain_idd6wsle1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.32 — Tubulin nucleotide-binding domain-like
Superfamily Superfamily superfamilyc.32.1 — Tubulin nucleotide-binding domain-like
Family Family familyc.32.1.1 — Tubulin, GTPase domain
Domain ID domain_idd6wsle2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.79 — Bacillus chorismate mutase-like
Superfamily Superfamily superfamilyd.79.2 — Tubulin C-terminal domain-like
Family Family familyd.79.2.1 — Tubulin, C-terminal domain
Domain ID domain_idd6wslf1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.32 — Tubulin nucleotide-binding domain-like
Superfamily Superfamily superfamilyc.32.1 — Tubulin nucleotide-binding domain-like
Family Family familyc.32.1.1 — Tubulin, GTPase domain
Domain ID domain_idd6wslf2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.79 — Bacillus chorismate mutase-like
Superfamily Superfamily superfamilyd.79.2 — Tubulin C-terminal domain-like
Family Family familyd.79.2.1 — Tubulin, C-terminal domain
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8. Citations (1)

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9. Files and Curves (10)