SAXSdb — 6o20

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

Transient receptor potential cation channel subfamily V member 5

Oryctolagus cuniculus

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 × 6 PDB declaration: hexameric（6） Consistent with protein copy count	Chain A； UniProt 1–730 Chain B； UniProt 1–730 Chain C； UniProt 1–730 Chain D； UniProt 1–730 Chain E； UniProt 1–730	Not recorded	Calmodulin × 1 （P62157） CA CALCIUM ION × 4	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.30 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 6O20	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
6B5V Structure of TRPV5 in complex with econazole Deposited 2017-09-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–730（730 aa） Chain B 1–730（730 aa） Chain C 1–730（730 aa） Chain D 1–730（730 aa）	Not recorded	ECL 1-[(2R)-2-[(4-chlorobenzyl)oxy]-2-(2,4-dichlorophenyl)ethyl]-1H-imidazole × 4 CA CALCIUM ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.80 Å
6DMR Lipid-bound full-length rbTRPV5 Deposited 2018-06-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–730（730 aa） Chain B 1–730（730 aa） Chain C 1–730（730 aa） Chain D 1–730（730 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.90 Å
6DMU PI(4,5)P2 bound full-length rbTRPV5 Deposited 2018-06-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–730（730 aa） Chain B 1–730（730 aa） Chain C 1–730（730 aa） Chain D 1–730（730 aa）	Not recorded	PIO [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phosphoryl]oxy-propyl] octanoate × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.00 Å
6DMW Calmodulin-bound full-length rbTRPV5 Deposited 2018-06-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 1–730（730 aa） Chain B 1–730（730 aa） Chain C 1–730（730 aa） Chain D 1–730（730 aa）	Not recorded	CA CALCIUM ION × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 8.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.40 Å
6O1N Cryo-EM structure of TRPV5 (1-660) in nanodisc Deposited 2019-02-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–730（730 aa） Chain B 1–730（730 aa） Chain C 1–730（730 aa） Chain D 1–730（730 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.90 Å
6O1P Cryo-EM structure of full length TRPV5 in nanodisc Deposited 2019-02-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–730（730 aa） Chain B 1–730（730 aa） Chain C 1–730（730 aa） Chain D 1–730（730 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.00 Å
6O1U Cryo-EM structure of TRPV5 W583A in nanodisc Deposited 2019-02-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–730（730 aa） Chain B 1–730（730 aa） Chain C 1–730（730 aa） Chain D 1–730（730 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.80 Å
6PBE ZINC17988990-bound TRPV5 in nanodiscs Deposited 2019-06-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–730（730 aa） Chain B 1–730（730 aa） Chain C 1–730（730 aa） Chain D 1–730（730 aa）	Not recorded	O6S (4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl)methyl 3-(3-oxo-2,3-dihydro-4H-1,4-benzoxazin-4-yl)propanoate × 8	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.78 Å
6PBF ZINC9155420-bound TRPV5 in nanodiscs Deposited 2019-06-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–730（730 aa） Chain B 1–730（730 aa） Chain C 1–730（730 aa） Chain D 1–730（730 aa）	Not recorded	O6V (1S)-1-(4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl)ethyl [(2S)-3-oxo-3,4-dihydro-2H-1,4-benzothiazin-2-yl]acetate × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.20 Å
7T6J Cryo-EM structure of TRPV5 at pH8 in nanodiscs Deposited 2021-12-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–730（730 aa） Chain B 1–730（730 aa） Chain C 1–730（730 aa） Chain D 1–730（730 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
7T6K Cryo-EM structure of TRPV5 at pH6 in nanodiscs Deposited 2021-12-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–730（730 aa） Chain B 1–730（730 aa） Chain C 1–730（730 aa） Chain D 1–730（730 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 6 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.00 Å
7T6L Cryo-EM structure of TRPV5 at pH5 in nanodiscs Deposited 2021-12-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–730（730 aa） Chain B 1–730（730 aa） Chain C 1–730（730 aa） Chain D 1–730（730 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.70 Å
7T6M Cryo-EM structure of TRPV5 in nanodiscs with PI(4,5)P2 at pH6 state 1 Deposited 2021-12-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–730（730 aa） Chain B 1–730（730 aa） Chain C 1–730（730 aa） Chain D 1–730（730 aa）	Not recorded	PIO [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phosphoryl]oxy-propyl] octanoate × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 6 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.80 Å
7T6N Cryo-EM structure of TRPV5 in nanodiscs at pH6 state 2 Deposited 2021-12-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–730（730 aa） Chain B 1–730（730 aa） Chain C 1–730（730 aa） Chain D 1–730（730 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 6 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.90 Å
7T6O Cryo-EM structure of TRPV5 in nanodiscs at pH6 state 3 Deposited 2021-12-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–730（730 aa） Chain B 1–730（730 aa） Chain C 1–730（730 aa） Chain D 1–730（730 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 6 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.60 Å
7T6P Cryo-EM structure of TRPV5 T709D in nanodiscs Deposited 2021-12-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–730（730 aa） Chain B 1–730（730 aa） Chain C 1–730（730 aa） Chain D 1–730（730 aa）	Mutation：T709D Mutation：T709D Mutation：T709D Mutation：T709D	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.80 Å
7T6Q Cryo-EM structure of TRPV5 T709D with PI(4,5)P2 in nanodiscs Deposited 2021-12-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–730（730 aa） Chain B 1–730（730 aa） Chain C 1–730（730 aa） Chain D 1–730（730 aa）	Mutation：T709D Mutation：T709D Mutation：T709D Mutation：T709D	PIO [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phosphoryl]oxy-propyl] octanoate × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.40 Å
7T6R Cryo-EM structure of TRPV5 T709D in nanodiscs in the presence of Calmodulin Deposited 2021-12-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–730（730 aa） Chain B 1–730（730 aa） Chain C 1–730（730 aa） Chain D 1–730（730 aa）	Mutation：T709D Mutation：T709D Mutation：T709D Mutation：T709D	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.00 Å
8FFN RR-bound wildtype rabbit TRPV5 in nanodiscs Deposited 2022-12-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–730（730 aa） Chain B 1–730（730 aa） Chain C 1–730（730 aa） Chain D 1–730（730 aa）	Not recorded	R2R ruthenium(6+) azanide pentaamino(oxido)ruthenium (1/4/2) × 1 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 8 ERG ERGOSTEROL × 8	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.96 Å
8FFO Cryo-EM structure of wildtype rabbit TRPV5 with PI(4,5)P2 in nanodiscs Deposited 2022-12-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–730（730 aa） Chain B 1–730（730 aa） Chain C 1–730（730 aa） Chain D 1–730（730 aa）	Not recorded	ERG ERGOSTEROL × 8 CPL 1-PALMITOYL-2-LINOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 16 PIO [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phosphoryl]oxy-propyl] octanoate × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.50 Å
8FFQ Wildtype rabbit TRPV5 into nanodiscs in the presence of PI(4,5)P2 and ruthenium red Deposited 2022-12-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–730（730 aa） Chain B 1–730（730 aa） Chain C 1–730（730 aa） Chain D 1–730（730 aa）	Not recorded	ERG ERGOSTEROL × 8 R2R ruthenium(6+) azanide pentaamino(oxido)ruthenium (1/4/2) × 1 CPL 1-PALMITOYL-2-LINOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.65 Å
8FHH Wildtype rabbit TRPV5 in nanodiscs in the presence of oleoyl coenzyme A, Closed stated Deposited 2022-12-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–730（730 aa） Chain B 1–730（730 aa） Chain C 1–730（730 aa） Chain D 1–730（730 aa）	Not recorded	POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 4 ERG ERGOSTEROL × 8	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.09 Å
8FHI Wildtype rabbit TRPV5 in nanodiscs in complex with oleoyl coenzyme A, Open stated Deposited 2022-12-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–730（730 aa） Chain B 1–730（730 aa） Chain C 1–730（730 aa） Chain D 1–730（730 aa）	Not recorded	ERG ERGOSTEROL × 8 3VV S-{(3R,5R,9R)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]-3,5,9-trihydroxy-8,8-dimethyl-3,5-dioxido-10,14-dioxo-2,4,6-trioxa-11,15-diaza-3lambda~5~,5lambda~5~-diphosphaheptadecan-17-yl} (9Z)-octadec-9-enethioate (non-preferred name) × 4 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.25 Å
8TF2 Wildtype rabbit TRPV5 into nanodiscs in Apo state Deposited 2023-07-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–730（730 aa） Chain B 1–730（730 aa） Chain C 1–730（730 aa） Chain D 1–730（730 aa）	Not recorded	ERG ERGOSTEROL × 8 CPL 1-PALMITOYL-2-LINOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 16	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.57 Å
8TF3 Wildtype rabbit TRPV5 into nanodiscs in complex with econazole Deposited 2023-07-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–730（730 aa） Chain B 1–730（730 aa） Chain C 1–730（730 aa） Chain D 1–730（730 aa）	Not recorded	ERG ERGOSTEROL × 8 CPL 1-PALMITOYL-2-LINOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 8 ECN 1-[(2S)-2-[(4-CHLOROBENZYL)OXY]-2-(2,4-DICHLOROPHENYL)ETHYL]-1H-IMIDAZOLE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.94 Å
8TF4 Wildtype rabbit TRPV5 into nanodiscs in the presence of PI(4,5)P2 and econazole Deposited 2023-07-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–730（730 aa） Chain B 1–730（730 aa） Chain C 1–730（730 aa） Chain D 1–730（730 aa）	Not recorded	ERG ERGOSTEROL × 8 CPL 1-PALMITOYL-2-LINOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 8 ECN 1-[(2S)-2-[(4-CHLOROBENZYL)OXY]-2-(2,4-DICHLOROPHENYL)ETHYL]-1H-IMIDAZOLE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.86 Å
9O6G Wildtype rabbit TRPV5 in nanodics in the presence of Menthol and PI(4,5)P2 Deposited 2025-04-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–730（730 aa） Chain B 1–730（730 aa） Chain C 1–730（730 aa） Chain D 1–730（730 aa）	Not recorded	ERG ERGOSTEROL × 8 CPL 1-PALMITOYL-2-LINOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 16 PIO [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phosphoryl]oxy-propyl] octanoate × 4 IT9 (-)-Isopiperitenone × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.37 Å

27 other PDB entries and 27 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	TRPV5_RABIT
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–730； UniProt 1–730 Author chain B； PDBConstruct 1–730； UniProt 1–730 Author chain C； PDBConstruct 1–730； UniProt 1–730 Author chain D； PDBConstruct 1–730； UniProt 1–730 Author chain E； PDBConstruct 1–730； UniProt 1–730

Calmodulin

Bos taurus

UniProt P62157

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 × 6 PDB declaration: hexameric（6） Consistent with protein copy count	Chain F； UniProt 1–149	Not recorded	Transient receptor potential cation channel subfamily V member 5 × 5 （Q9XSM3） CA CALCIUM ION × 4	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.30 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 6O20	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1A29 CALMODULIN COMPLEXED WITH TRIFLUOPERAZINE (1:2 COMPLEX) Deposited 1998-01-19	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–148（148 aa）	Not recorded	CA CALCIUM ION × 4 TFP 10-[3-(4-METHYL-PIPERAZIN-1-YL)-PROPYL]-2-TRIFLUOROMETHYL-10H-PHENOTHIAZINE × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 5；PROTEIN WAS CRYSTALLIZED BY SITTING DROP TECHNIQUE IN THE COLD ROOM (8 DEGREES C +/- 2 DEGREES C) BY MIXING 4 MICROLITERS OF 1 MM PROTEIN CONTAINING 1.2-1.5 MM TFP IN 5 MM CACL2 WITH 4 MICROLITERS OF THE RESERVOIR SOLUTION (1 ML 10 MM SODIUM CACODYLATE/HCL BUFFER, PH 5.2-5.6 WITH 10 MM CACL2, 25-30 % (W/V) POLYETHYLENE GLYCOL 6000), CRYSTAL GROWTH TOOK 2-3 WEEKS., pH 5.0	Resolution 2.74 Å R-free 0.265
1AK8 NMR SOLUTION STRUCTURE OF CERIUM-LOADED CALMODULIN AMINO-TERMINAL DOMAIN (CE2-TR1C), 23 STRUCTURES Deposited 1997-05-29	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–75（75 aa） Fragment：N-TERMINAL DOMAIN, TR1C	Not recorded	CE CERIUM (III) ION × 2	SOLUTION NMR NMR measurement conditions pH 6；298 K	Resolution not provided
1CDM MODULATION OF CALMODULIN PLASTICITY IN MOLECULAR RECOGNITION ON THE BASIS OF X-RAY STRUCTURES Deposited 1993-10-08	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 4–147（144 aa）	Not recorded	CA CALCIUM ION × 4	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.00 Å
1CMF NMR SOLUTION STRUCTURE OF APO CALMODULIN CARBOXY-TERMINAL DOMAIN Deposited 1995-07-19	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 76–148（73 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
1CMG NMR SOLUTION STRUCTURE OF CALCIUM-LOADED CALMODULIN CARBOXY-TERMINAL DOMAIN Deposited 1995-07-19	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 76–148（73 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
1FW4 CRYSTAL STRUCTURE OF E. COLI FRAGMENT TR2C FROM CALMODULIN TO 1.7 A RESOLUTION Deposited 2000-09-21	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 78–148（71 aa） Fragment：C-TERMINAL DOMAIN (RESIDUES 78-148)	Not recorded	CA CALCIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；293 K；PEG 4000, calcium chloride, sodium acetate, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 1.70 Å R-free 0.220
1LIN CALMODULIN COMPLEXED WITH TRIFLUOPERAZINE (1:4 COMPLEX) Deposited 1995-10-11	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–148（148 aa）	Not recorded	CA CALCIUM ION × 4 TFP 10-[3-(4-METHYL-PIPERAZIN-1-YL)-PROPYL]-2-TRIFLUOROMETHYL-10H-PHENOTHIAZINE × 4	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.00 Å
1PRW Crystal structure of bovine brain Ca++ calmodulin in a compact form Deposited 2003-06-20	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–148（148 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	CA CALCIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.4；296 K；PEG 6000, sodium acetate, glycerol, pH 5.4, VAPOR DIFFUSION, HANGING DROP, temperature 296K	Resolution 1.70 Å R-free 0.230
1XA5 Structure of Calmodulin in complex with KAR-2, a bis-indol alkaloid Deposited 2004-08-25	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–148（148 aa）	Not recorded	CA CALCIUM ION × 4 KAR 3"-(BETA-CHLOROETHYL)-2",4"-DIOXO-3, 5"-SPIRO-OXAZOLIDINO-4-DEACETOXY-VINBLASTINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.7；279 K；CaCl2, MgCl2, cacodylate, PEG 8000, pH 4.7, VAPOR DIFFUSION, HANGING DROP, temperature 279K	Resolution 2.12 Å R-free 0.261
2F2O Structure of calmodulin bound to a calcineurin peptide: a new way of making an old binding mode Deposited 2005-11-17	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 Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 0–148（149 aa） Chain B 0–148（149 aa）	Not recorded	CA CALCIUM ION × 8	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.17 Å R-free 0.289
2F2O Structure of calmodulin bound to a calcineurin peptide: a new way of making an old binding mode Deposited 2005-11-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Insufficient information Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 0–148（149 aa） Chain B 0–148（149 aa）	Not recorded	CA CALCIUM ION × 16	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.17 Å R-free 0.289
2F2P Structure of calmodulin bound to a calcineurin peptide: a new way of making an old binding mode Deposited 2005-11-17	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 Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 0–148（149 aa） Chain B 0–148（149 aa）	Not recorded	CA CALCIUM ION × 8	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.60 Å R-free 0.297
2F2P Structure of calmodulin bound to a calcineurin peptide: a new way of making an old binding mode Deposited 2005-11-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Insufficient information Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 0–148（149 aa） Chain B 0–148（149 aa）	Not recorded	CA CALCIUM ION × 16	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.60 Å R-free 0.297
2FOT Crystal structure of the complex between calmodulin and alphaII-spectrin Deposited 2006-01-13	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–148（148 aa）	Not recorded	CA CALCIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；298 K；50mM Tris,pH 8.00, 30% PEG 8000, 0.1M ammonium-sulfate, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 2.45 Å R-free 0.269
3IF7 Structure of Calmodulin complexed with its first endogenous inhibitor, sphingosylphosphorylcholine Deposited 2009-07-24	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–149（148 aa）	Not recorded	CA CALCIUM ION × 4 SPU 2-{[(R)-{[(2S,3R,4E)-2-amino-3-hydroxyoctadec-4-en-1-yl]oxy}(hydroxy)phosphoryl]oxy}-N,N,N-trimethylethanaminium × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；293 K；50mM sodium cacodylate, 10mM CaCl2, 10mM MgCl2, 28% PEG 8000: Mixed with 10mM lipid in methanol solution and 1mM protein solution, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 1.60 Å R-free 0.238

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

View Construct and Data Evidence

UniProt name	CALM_BOVIN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain F； PDBConstruct 21–169； UniProt 1–149

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	6o20
Deposition date deposition_date	2019-02-22
Structure title title	Cryo-EM structure of TRPV5 with calmodulin bound
Keywords keywords	TRP channel, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method method	ELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier	46.56 Å
Radius of gyration Rg (electron density) rg_electron	45.57 Å
Forward intensity I(0) i0	1206110000.00
Molecular weight molecular_weight	297940.0 kDa
Excluded volume excluded_volume	376700 Å³
Envelope volume envelope_volume	523280 Å³
Hydration-shell volume shell_volume	92032 Å³
Envelope diameter envelope_diameter	146.5 Å
Shell Rg shell_rg	53.33 Å
Envelope Rg envelope_rg	44.62 Å
Shape Rg shape_rg	45.57 Å
Total Rg total_rg	45.88 Å
Total atoms total_atoms	20950
Residues n_residues	2624
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

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

Maximum dimension Dmax dmax	140.9 Å
Rg (real space) rg_real	46.19 Å
Rg uncertainty (real space) rg_real_error	0.78 Å
I(0) (real space) i0_real	1.2060e+09
I(0) uncertainty (real space) i0_real_error	2.1540e+07
Rg (reciprocal space) rg_reciprocal	46.56 Å
I(0) (reciprocal space) i0_reciprocal	1207000000.0000
Solution quality estimate total_estimate	0.8918
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	58.0 Å
Skewness Skewness skewness	0.017
Kurtosis Kurtosis kurtosis	-0.563
Angular range angular_range	— – 0.1700 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	75430000.0000
Real-space data points n_real_points	35
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.932; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.960; Smooth: 0.833

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	Transient receptor potential cation channel subfamily V member 5
Molecular weight formula_weight	82899.7 kDa
Source method src_method	man
Copy count entity_count	5

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,E,B,C,D
Atom count atom_count	20950

MGACPPKAKGPWAQLQKLLISWPVGEQDWEQYRDRVNMLQQERIRDSPLLQAAKENDLRLLKILLLNQSCDFQQRGAVGETALHVAALYDNLEAATLLMEAAPELAKEPALCEPFVGQTALHIAVMNQNLNLVRALLARGASVSARATGAAFRRSPHNLIYYGEHPLSFAACVGSEEIVRLLIEHGADIRAQDSLGNTVLHILILQPNKTFACQMYNLLLSYDEHSDHLQSLELVPNHQGLTPFKLAGVEGNTVMFQHLMQKRKHVQWTCGPLTSTLYDLTEIDSWGEELSFLELVVSSKKREARQILEQTPVKELVSFKWKKYGRPYFCVLASLYILYMICFTTCCIYRPLKLRDDNRTDPRDITILQQKLLQEAYVTHQDNIRLVGELVTVTGAVIILLLEIPDIFRVGASRYFGQTILGGPFHVIIITYASLVLLTMVMRLTNMNGEVVPLSFALVLGWCSVMYFARGFQMLGPFTIMIQKMIFGDLMRFCWLMAVVILGFASAFHITFQTEDPNNLGEFSDYPTALFSTFELFLTIIDGPANYSVDLPFMYCITYAAFAIIATLLMLNLFIAMMGDTHWRVAQERDELWRAQVVATTVMLERKMPRFLWPRSGICGYEYGLGDRWFLRVENHHDQNPLRVLRYVEAFKCSDKEDGQEQLSEKRPSTVESGMLSRASVAFQTPSLSRTTSQSSNSHRGWEILRRNTLGHLNLGLDLGEGDGEEVYHF

来源 Source

来源生物 organism	Oryctolagus cuniculus
通用名 common_name	Rabbit
NCBI Class编号 ncbi_taxonomy_id	9986
宿主生物 host_organism	Homo sapiens

Entity 2 Entity 2 polymer

Description description	Calmodulin
Molecular weight formula_weight	19023.9 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	F

MGSSHHHHHHSSGLVPRGSHMADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAK

来源 Source

来源生物 organism	Bos taurus
通用名 common_name	Bovine
NCBI Class编号 ncbi_taxonomy_id	9913
宿主生物 host_organism	Escherichia coli-Pichia pastoris shuttle vector pPpARG4

Entity 3 Entity 3 non-polymer

Description description	CALCIUM ION
Molecular weight formula_weight	40.1 kDa
Source method src_method	syn
Copy count entity_count	4

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7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id	6o20A01
Class class	1 — Mainly Alpha
Architecture architecture	25 — Alpha Horseshoe
Topology topology	40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily	20 — Ankyrin repeat-containing domain

Domain ID domain_id	6o20B01
Class class	1 — Mainly Alpha
Architecture architecture	25 — Alpha Horseshoe
Topology topology	40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily	20 — Ankyrin repeat-containing domain

Domain ID domain_id	6o20C01
Class class	1 — Mainly Alpha
Architecture architecture	25 — Alpha Horseshoe
Topology topology	40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily	20 — Ankyrin repeat-containing domain

Domain ID domain_id	6o20D01
Class class	1 — Mainly Alpha
Architecture architecture	25 — Alpha Horseshoe
Topology topology	40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily	20 — Ankyrin repeat-containing domain

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8. Citations (1)

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	1

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Resolution resolution	3.30 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	34604

fit	/app/data/saxs_computation/o2/6o20/6o20.fit
pddf	/app/data/pr_computation/o2/6o20/6o20.pr.out
profile	/app/data/saxs_computation/o2/6o20/6o20.dat

Cryo-EM structure of TRPV5 with calmodulin bound

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

Transient receptor potential cation channel subfamily V member 5

State in the Current Structure

Other States of the Same Protein in the Database

Calmodulin

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

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 non-polymer

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)