SAXSdb — 3err

▼

1. Protein Identity and Related Structures Protein Identity & Related Structures

fusion protein of microtubule binding domain from mouse cytoplasmic dynein and seryl-tRNA synthetase from Thermus thermophilus

Thermus thermophilus

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 94–419 Chain B； UniProt 94–419	Mutation：C3323A, C3387A	AMP ADENOSINE MONOPHOSPHATE × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；300 K；Protein was changed into crystallization buffer (20mM K-HEPES, pH7.5, 10% w/v glycerol, 0.2mM PMSF, 1mM DTT, 4mM Mg-ATP, 0.01% Na-Azide) and concentrated to 18 mg/ml. Crystallization was carried out by setting hanging drops containing 2 ul of protein, (diluted to 13.5mg/ml with 20mM K-Hepes, pH 7.5, 10% glycerol), 0.3 ul 70% glycerol and 1.8 ul of precipitant (20% PEG 4000, 200mM Ammonium sulfate, 100mM Bis-Tris, pH 5.5) over 500ml of the same precipitant solution. Crystals appeared within one day and were of dimensions up to 200 um., VAPOR DIFFUSION, HANGING DROP, temperature 300K	Resolution 2.27 Å R-free 0.247

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 3ERR	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1SER THE 2.9 ANGSTROMS CRYSTAL STRUCTURE OF T. THERMOPHILUS SERYL-TRNA SYNTHETASE COMPLEXED WITH TRNA SER Deposited 1994-02-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Homooligomer；Protein × 2 PDB declaration: trimeric	Chain A 1–421（421 aa） Chain B 1–421（421 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.90 Å
1SES CRYSTAL STRUCTURES AT 2.5 ANGSTROMS RESOLUTION OF SERYL-TRNA SYNTHETASE COMPLEXED WITH TWO DIFFERENT ANALOGUES OF SERYL-ADENYLATE Deposited 1994-02-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–421（421 aa） Chain B 1–421（421 aa）	Not recorded	AHX SERYL-HYDROXAMATE-ADENOSINE MONOPHOSPHATE × 1 AMP ADENOSINE MONOPHOSPHATE × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.50 Å
1SET CRYSTAL STRUCTURES AT 2.5 ANGSTROMS RESOLUTION OF SERYL-TRNA SYNTHETASE COMPLEXED WITH TWO DIFFERENT ANALOGUES OF SERYL-ADENYLATE Deposited 1994-02-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–421（421 aa） Chain B 1–421（421 aa）	Not recorded	SSA 5'-O-(N-(L-SERYL)-SULFAMOYL)ADENOSINE × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.55 Å
1SRY REFINED CRYSTAL STRUCTURE OF THE SERYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS AT 2.5 ANGSTROMS RESOLUTION Deposited 1993-08-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–421（421 aa） Chain B 1–421（421 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.50 Å
5EIU Mini TRIM5 B-box 2 dimer C2 crystal form Deposited 2015-10-30	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 49–78（30 aa） Fragment：TRIM5 B-box 2 Chain D 49–78（30 aa） Fragment：TRIM5 B-box 2	Not recorded	ZN ZINC ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；290 K；0.1M Tris 7.0, 0.2M NaCl, 28% PEG3350, + (0.025% w/v Ala-ala, 0.025% w/v Ala-gly, 0.025% w/v Gly-gly-gly-gly, 0.025% w/v Leu-gly-gly from silver bullet)	Resolution 1.91 Å R-free 0.217
5EIU Mini TRIM5 B-box 2 dimer C2 crystal form Deposited 2015-10-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain A 49–78（30 aa） Fragment：TRIM5 B-box 2	Not recorded	ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；290 K；0.1M Tris 7.0, 0.2M NaCl, 28% PEG3350, + (0.025% w/v Ala-ala, 0.025% w/v Ala-gly, 0.025% w/v Gly-gly-gly-gly, 0.025% w/v Leu-gly-gly from silver bullet)	Resolution 1.91 Å R-free 0.217
5EIU Mini TRIM5 B-box 2 dimer C2 crystal form Deposited 2015-10-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain D 49–78（30 aa） Fragment：TRIM5 B-box 2	Not recorded	ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；290 K；0.1M Tris 7.0, 0.2M NaCl, 28% PEG3350, + (0.025% w/v Ala-ala, 0.025% w/v Ala-gly, 0.025% w/v Gly-gly-gly-gly, 0.025% w/v Leu-gly-gly from silver bullet)	Resolution 1.91 Å R-free 0.217
5F7T TRIM5 B-box2 and coiled-coil chimera Deposited 2015-12-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain E 49–78（30 aa）	Not recorded	ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；290 K；0.1M NaAcetate 4.6, 0.2M CaAcetate, 23% PEG 3350	Resolution 2.29 Å R-free 0.256
5F7T TRIM5 B-box2 and coiled-coil chimera Deposited 2015-12-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain F 49–78（30 aa）	Not recorded	ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；290 K；0.1M NaAcetate 4.6, 0.2M CaAcetate, 23% PEG 3350	Resolution 2.29 Å R-free 0.256
5F7T TRIM5 B-box2 and coiled-coil chimera Deposited 2015-12-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain H 49–78（30 aa）	Not recorded	ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；290 K；0.1M NaAcetate 4.6, 0.2M CaAcetate, 23% PEG 3350	Resolution 2.29 Å R-free 0.256
5F7T TRIM5 B-box2 and coiled-coil chimera Deposited 2015-12-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain L 49–78（30 aa）	Not recorded	ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；290 K；0.1M NaAcetate 4.6, 0.2M CaAcetate, 23% PEG 3350	Resolution 2.29 Å R-free 0.256
5IEA TRIM5 B-box2 and coiled-coil chimera Deposited 2016-02-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 49–78（30 aa） Chain B 49–78（30 aa） Chain D 49–78（30 aa）	Not recorded	ZN ZINC ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 6.6；310 K；0.1 M HEPES pH 6.6 0.25 M NaCl 25% PEG 3350	Resolution 3.26 Å R-free 0.304
5IEA TRIM5 B-box2 and coiled-coil chimera Deposited 2016-02-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Insufficient information Homooligomer；Protein × 3 PDB declaration: trimeric	Chain C 49–78（30 aa） Chain F 49–78（30 aa） Chain K 49–78（30 aa）	Not recorded	ZN ZINC ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 6.6；310 K；0.1 M HEPES pH 6.6 0.25 M NaCl 25% PEG 3350	Resolution 3.26 Å R-free 0.304
5VA4 TRIM-Cyclophilin A B-box 2 and coiled-coil chimera Deposited 2017-03-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 49–78（30 aa）	Not recorded	ZN ZINC ION × 9	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；290 K；17% PEG 3350, 0.4 M sodium/potassium tartrate	Resolution 2.31 Å R-free 0.287
9QRP Thermus thermophilus seryl-tRNA synthetase bound to tRNA(ser)(GGA) and seryl-adenylate analogue. Deposited 2025-04-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Homooligomer；Protein × 2 PDB declaration: trimeric	Chain A 1–421（421 aa） Chain B 1–421（421 aa）	Not recorded	SSA 5'-O-(N-(L-SERYL)-SULFAMOYL)ADENOSINE × 2 SO4 SULFATE ION × 10 MN MANGANESE (II) ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.2；293 K；10 microliter hanging drops containing 25 mM Tris-maleate/NaOH buffer at pH 7.2,2.5 mM MgC12,20% saturated (V/V) ammonium sulphate, 1 mM NaN3, 2.6 mg/ml tRNA(ser) and 5.6 mg/ml seryl-tRNA synthetase (stoichiometric ratio of 1.5 tRNA molecules to one enzyme dimer), were equil- ibrated at room temperature against 32% saturated ammonium sulphate.	Resolution 2.70 Å R-free 0.230

9 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	SYS_THET2
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 203–528； UniProt 94–419 Author chain B； PDBConstruct 203–528； UniProt 94–419

fusion protein of microtubule binding domain from mouse cytoplasmic dynein and seryl-tRNA synthetase from Thermus thermophilus

Thermus thermophilus

UniProt Q9JHU4

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 3260–3427 Chain B； UniProt 3260–3427	Mutation：C3323A, C3387A	AMP ADENOSINE MONOPHOSPHATE × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；300 K；Protein was changed into crystallization buffer (20mM K-HEPES, pH7.5, 10% w/v glycerol, 0.2mM PMSF, 1mM DTT, 4mM Mg-ATP, 0.01% Na-Azide) and concentrated to 18 mg/ml. Crystallization was carried out by setting hanging drops containing 2 ul of protein, (diluted to 13.5mg/ml with 20mM K-Hepes, pH 7.5, 10% glycerol), 0.3 ul 70% glycerol and 1.8 ul of precipitant (20% PEG 4000, 200mM Ammonium sulfate, 100mM Bis-Tris, pH 5.5) over 500ml of the same precipitant solution. Crystals appeared within one day and were of dimensions up to 200 um., VAPOR DIFFUSION, HANGING DROP, temperature 300K	Resolution 2.27 Å R-free 0.247

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 3ERR	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
3J1T High affinity dynein microtubule binding domain - tubulin complex Deposited 2012-06-25	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 3264–3427（164 aa） Fragment：SEE REMARK 999	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 50 mM Tris HCl, 1 mM MgCl2, 1mM EGTA, 1mM DTT；pH 8；50 mM Tris HCl, 1 mM MgCl2, 1mM EGTA, 1mM DTT cryo-EM vitrification conditions Cryogen ETHANE；The solution was blotted manually, and the process of addition and blotting of SRS-MTBD was repeated a total of three times. The final blotting was done inside the humidity chamber of a Vitrobot Mark IV (FEI) at 22 Celsius.	Resolution 9.70 Å
3J1U Low affinity dynein microtubule binding domain - tubulin complex Deposited 2012-06-25	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 3264–3427（164 aa） Fragment：SEE REMARK 999	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 50 mM Tris HCl, 1 mM MgCl2, 1mM EGTA, 1mM DTT；pH 8；50 mM Tris HCl, 1 mM MgCl2, 1mM EGTA, 1mM DTT cryo-EM vitrification conditions Cryogen ETHANE；The solution was blotted manually, and the process of addition and blotting of SRS-MTBD was repeated a total of three times. The final blotting was done inside the humidity chamber of a Vitrobot Mark IV (FEI) at 22 Celsius.	Resolution 9.70 Å
3WUQ Structure of the entire stalk region of the dynein motor domain Deposited 2014-05-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 3207–3483（277 aa） Fragment：STALK DOMAIN, UNP residues 3207-3483	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；20% PEG3350, 0.2M ammonium phosphate, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 3.50 Å R-free 0.305
5AYH Structure of the entire dynein stalk region Deposited 2015-08-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 3207–3475（269 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；PEG 3350, ammonium phosphate monobasic	Resolution 3.01 Å R-free 0.295
6RZA Cryo-EM structure of the human inner arm dynein DNAH7 microtubule binding domain bound to microtubules Deposited 2019-06-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 5 PDB declaration: pentameric	Chain X 3270–3284（15 aa） Chain X 3410–3418（9 aa）	Not recorded	GTP GUANOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 2 TA1 TAXOL × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.50 Å

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	DYHC1_MOUSE
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 35–202； UniProt 3260–3427 Author chain B； PDBConstruct 35–202； UniProt 3260–3427

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	3err
Deposition date deposition_date	2008-10-03
Structure title title	Microtubule binding domain from mouse cytoplasmic dynein as a fusion with seryl-tRNA synthetase
Keywords keywords	dynein, microtubule binding domain, coiled coil, fusion protein, LIGASE; LIGASE
Experimental Method method	X-RAY DIFFRACTION

▼

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	41.02 Å
Radius of gyration Rg (electron density) rg_electron	41.02 Å
Forward intensity I(0) i0	218697000.00
Molecular weight molecular_weight	120150.0 kDa
Excluded volume excluded_volume	150840 Å³
Envelope volume envelope_volume	221230 Å³
Hydration-shell volume shell_volume	47198 Å³
Envelope diameter envelope_diameter	133.4 Å
Shell Rg shell_rg	43.64 Å
Envelope Rg envelope_rg	40.59 Å
Shape Rg shape_rg	40.95 Å
Total Rg total_rg	41.43 Å
Total atoms total_atoms	8466
Residues n_residues	1054
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

▼

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	127.2 Å
Rg (real space) rg_real	41.03 Å
Rg uncertainty (real space) rg_real_error	0.87 Å
I(0) (real space) i0_real	2.1870e+08
I(0) uncertainty (real space) i0_real_error	3.4970e+06
Rg (reciprocal space) rg_reciprocal	41.02 Å
I(0) (reciprocal space) i0_reciprocal	218700000.0000
Solution quality estimate total_estimate	0.8558
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	32.6 Å
Skewness Skewness skewness	0.158
Kurtosis Kurtosis kurtosis	-0.846
Angular range angular_range	— – 0.1950 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	26550000.0000
Real-space data points n_real_points	40
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.881; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.915; Smooth: 0.563

▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	fusion protein of microtubule binding domain from mouse cytoplasmic dynein and seryl-tRNA synthetase from Thermus thermophilus
Molecular weight formula_weight	60957.7 kDa
Mutation mutation	C3323A, C3387A
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	8589

MVDLKRLRQEPEVFHRAIREKGVALDLEALLAVDEQLHKQQEVIADKQMSVKEDLDKVEPAVIEAQNAVKSIKKQHLVEVRSMANPPAAVKLALESIALLLGESTTDWKQIRSIIMRENFIPTIVNFSAEEISDAIREKMKKNYMSNPSYNYEIVNRASLAAGPMVKWAIAQLNYADMLKRVEPLRNELQKLEDDAKDNQQKLEALLLQVPLPPWPGAPVGGEEANREIKRVGGPPEFSFPPLDHVALMEKNGWWEPRISQVSGSRSYALKGDLALYELALLRFAMDFMARRGFLPMTLPSYAREKAFLGTGHFPAYRDQVWAIAETDLYLTGTAEVVLNALHSGEILPYEALPLRYAGYAPAFRSEAGSFGKDVRGLMRVHQFHKVEQYVLTEASLEASDRAFQELLENAEEILRLLELPYRLVEVATGDMGPGKWRQVDIEVYLPSEGRYRETHSCSALLDWQARRANLRYRDPEGRVRYAYTLNNTALATPRILAMLLENHQLQDGRVRVPQALIPYMGKEVLEPGAHHHHHH

来源 Source

来源生物 organism	Thermus thermophilus
NCBI Class编号 ncbi_taxonomy_id	262724
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	ADENOSINE MONOPHOSPHATE
Molecular weight formula_weight	347.2 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	123

▼

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id	3errA01
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	920 — Histone Acetyltransferase; Chain A
Homologous superfamily homologous superfamily	60 —

Domain ID domain_id	3errA02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	930 — BirA Bifunctional Protein; domain 2
Homologous superfamily homologous superfamily	10 — Bira Bifunctional Protein; Domain 2

Domain ID domain_id	3errB01
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	920 — Histone Acetyltransferase; Chain A
Homologous superfamily homologous superfamily	60 —

Domain ID domain_id	3errB02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	930 — BirA Bifunctional Protein; domain 2
Homologous superfamily homologous superfamily	10 — Bira Bifunctional Protein; Domain 2

▶

8. Citations (1)

▶

Unit-cell length a length_a	144.302 Å
Unit-cell length b length_b	144.302 Å
Unit-cell length c length_c	159.946 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	18

Space group space_group	H 3
Space-group number int_tables_number	146
Crystal system crystal_system	—

Resolution resolution	2.270 Å
Low-resolution limit resolution_low	49.270 Å
R factor r_factor	0.1995
R_work r_work	0.1970
R_free r_free	0.2465

fit	/app/data/saxs_computation/er/3err/3err.fit
pddf	/app/data/pr_computation/er/3err/3err.pr.out
profile	/app/data/saxs_computation/er/3err/3err.dat

Microtubule binding domain from mouse cytoplasmic dynein as a fusion with seryl-tRNA synthetase

1. Protein Identity and Related Structures Protein Identity & Related Structures

fusion protein of microtubule binding domain from mouse cytoplasmic dynein and seryl-tRNA synthetase from Thermus thermophilus

State in the Current Structure

Other States of the Same Protein in the Database

fusion protein of microtubule binding domain from mouse cytoplasmic dynein and seryl-tRNA synthetase from Thermus thermophilus

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)