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Protein Structures and Oligomeric States

Enter a protein name, UniProt accession or PDB ID. Name searches ask you to confirm the protein identity before related structures are queried.

Current Protein Identity：P51681 New Search
20PDB entries
27Biological assembly
45chain/assembly records
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics

Difference tags compare only the current result set; every original PDB and assembly record remains separate.

Related-Structure Differences

Each row represents one biological assembly in one PDB entry; multiple monomers of the same protein are listed separately.

PDB Entry Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Experimental Method Experimental Conditions Structure Quality
2L87 The 27-residue N-terminus CCR5-peptide in a ternary complex with HIV-1 gp120 and a CD4-mimic peptide Deposited 2011-01-06 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 1–27（27 aa） Fragment：N-terminal domain, residues 1-27
Mutation：C20A Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7；Ionic strength (raw mmCIF value) 300
NMR sample composition 1mM Nt-CCR5; 0.1mM gp120/CD4mimic; 95% H2O/5% D2O | 95% H2O/5% D2O
Resolution not provided
2MZX CCR5-ECL2 helical structure, residues Q186-T195 Deposited 2015-02-26 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 186–195（10 aa） Fragment：Extracellular domain residues 186-195
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 4.8；277 K；Ionic strength (raw mmCIF value) 0；Pressure ambient
NMR sample composition 20 mM [U-99% 2H] acetic acid, 0.005 % v/v Thiomersal, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
2RLL CCR5 Nt(7-15) Deposited 2007-07-21 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 7–15（9 aa） Fragment：Extracellular domain, UNP residues 7-15
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.8；300 K；Ionic strength (raw mmCIF value) 50mM NaCl；Pressure ambient
NMR sample composition 800uM protein; 90% H2O, 10% D2O | 90% H2O/10% D2O
Resolution not provided
2RRS NMR Structure of LC4 transmembrane segment of CCR5 Deposited 2011-04-11 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 157–174（18 aa） Fragment：LC4 transmembrane segment, UNP residues 157-174
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 4.5；293 K；Ionic strength (raw mmCIF value) 280；Pressure ambient
NMR sample composition 2 mM LC4-1, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
4MBS Crystal Structure of the CCR5 Chemokine Receptor Deposited 2013-08-19 Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 2–223（222 aa） Fragment：Rubredoxin inserted into CCR5 between residue 223 and 227
Chain A 227–352（126 aa） Fragment：Rubredoxin inserted into CCR5 between residue 223 and 227
Mutation：C58Y, G163N, A233D, K303E Mutation：C58Y, G163N, A233D, K303E MRV 4,4-difluoro-N-[(1S)-3-{(3-exo)-3-[3-methyl-5-(propan-2-yl)-4H-1,2,4-triazol-4-yl]-8-azabicyclo[3.2.1]oct-8-yl}-1-phenylpropyl]cyclohexanecarboxamide × 1 ZN ZINC ION × 1 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 6 X-RAY DIFFRACTION
X-ray crystallization conditions LIPIDIC CUBIC PHASE；pH 7；293 K；32% PEG 400, 0.1M HEPES, 0.1M sodium chloride, pH 7.0, Lipidic cubic phase, temperature 293K
Resolution 2.71 Å R-free 0.263
4MBS Crystal Structure of the CCR5 Chemokine Receptor Deposited 2013-08-19 Assembly 2 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain B 2–223（222 aa） Fragment：Rubredoxin inserted into CCR5 between residue 223 and 227
Chain B 227–352（126 aa） Fragment：Rubredoxin inserted into CCR5 between residue 223 and 227
Mutation：C58Y, G163N, A233D, K303E Mutation：C58Y, G163N, A233D, K303E MRV 4,4-difluoro-N-[(1S)-3-{(3-exo)-3-[3-methyl-5-(propan-2-yl)-4H-1,2,4-triazol-4-yl]-8-azabicyclo[3.2.1]oct-8-yl}-1-phenylpropyl]cyclohexanecarboxamide × 1 ZN ZINC ION × 1 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 4 X-RAY DIFFRACTION
X-ray crystallization conditions LIPIDIC CUBIC PHASE；pH 7；293 K；32% PEG 400, 0.1M HEPES, 0.1M sodium chloride, pH 7.0, Lipidic cubic phase, temperature 293K
Resolution 2.71 Å R-free 0.263
5UIW Crystal Structure of CC Chemokine Receptor 5 (CCR5) in complex with high potency HIV entry inhibitor 5P7-CCL5 Deposited 2017-01-15 Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 2–223（222 aa）
Chain A 227–352（126 aa）
Mutation：C58Y, G163N, A233D, K303E Mutation：C58Y, G163N, A233D, K303E ZN ZINC ION × 1 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 6 OLA OLEIC ACID × 2 X-RAY DIFFRACTION
X-ray crystallization conditions LIPIDIC CUBIC PHASE；pH 6.3；295.5 K；29% (v/v) PEG 400, 120 mM lithium citrate, 1.2% (w/v) 1,5-Diaminopentane dihydrochloride, 100 mM 2-(N-morpholino)ethanesulfonic acid
Resolution 2.20 Å R-free 0.250
5YY4 Crystal structure of the scFv antibody 4B08 with sulfated epitope peptide Deposited 2017-12-07 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain B 11–19（9 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) SO4 SULFATE ION × 2 CL CHLORIDE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.8；293.15 K；100mM sodium acetate, 1.4M Ammonium sulfate, pH 4.8
Resolution 1.59 Å R-free 0.194
6AKX The Crystal structure of Human Chemokine Receptor CCR5 in complex with compound 21 Deposited 2018-09-04 Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 2–223（222 aa）
Chain A 227–319（93 aa）
Mutation：C58Y, G163N, A233D, K303E Mutation：C58Y, G163N, A233D, K303E ZN ZINC ION × 1 NO3 NITRATE ION × 1 A4R N-[(1S)-3-{(3-exo)-3-[3-methyl-5-(propan-2-yl)-4H-1,2,4-triazol-4-yl]-8-azabicyclo[3.2.1]octan-8-yl}-1-(thiophen-2-yl)propyl]cyclopentanecarboxamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions LIPIDIC CUBIC PHASE；293.15 K；PEG 400, HEPES pH 7.5, ammonium acetate
Resolution 2.80 Å R-free 0.269
6AKX The Crystal structure of Human Chemokine Receptor CCR5 in complex with compound 21 Deposited 2018-09-04 Assembly 2 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain B 2–223（222 aa）
Chain B 227–319（93 aa）
Mutation：C58Y, G163N, A233D, K303E Mutation：C58Y, G163N, A233D, K303E ZN ZINC ION × 1 NO3 NITRATE ION × 1 A4R N-[(1S)-3-{(3-exo)-3-[3-methyl-5-(propan-2-yl)-4H-1,2,4-triazol-4-yl]-8-azabicyclo[3.2.1]octan-8-yl}-1-(thiophen-2-yl)propyl]cyclopentanecarboxamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions LIPIDIC CUBIC PHASE；293.15 K；PEG 400, HEPES pH 7.5, ammonium acetate
Resolution 2.80 Å R-free 0.269
6AKY The Crystal structure of Human Chemokine Receptor CCR5 in complex with compound 34 Deposited 2018-09-04 Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 2–223（222 aa）
Chain A 227–319（93 aa）
Mutation：C58Y, G163N, A233D, K303E Mutation：C58Y, G163N, A233D, K303E ZN ZINC ION × 1 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 1 A4X 4,4-difluoro-N-[(1S)-3-{(3-exo)-3-[3-methyl-5-(propan-2-yl)-4H-1,2,4-triazol-4-yl]-8-azabicyclo[3.2.1]octan-8-yl}-1-(thiophen-3-yl)propyl]cyclohexane-1-carboxamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions LIPIDIC CUBIC PHASE；293 K；PEG400, HEPES, ammonium acetate
Resolution 2.80 Å R-free 0.283
6FGP NMR solution structure of monomeric CCL5 in complex with a doubly-sulfated N-terminal segment of CCR5 Deposited 2018-01-11 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 1–27（27 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 4.8；310 K；Ionic strength (raw mmCIF value) 130；Pressure 1
NMR measurement conditions pH 4.8；310 K；Ionic strength (raw mmCIF value) 130；Pressure 1
NMR measurement conditions pH 4.8；310 K；Ionic strength (raw mmCIF value) 130；Pressure 1
NMR sample composition 120 uM [U-15N] CCL5(P9S)/Nt-CCR5(1-27), 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 120 uM [U-13C] CCL5(P9S)/Nt-CCR5(1-27), 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 120 uM U-15N;13C CCL5(P9S)/Nt-CCR5(1-27), 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
6MEO Structural basis of coreceptor recognition by HIV-1 envelope spike Deposited 2018-09-06 Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain B 1–313（313 aa） Fragment：residues 1-313
Non-standard monomer：Yes (specific site not provided by mmCIF) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 7 BMA beta-D-mannopyranose × 1 A2G 2-acetamido-2-deoxy-alpha-D-galactopyranose × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 8；100 mM Tris-HCl, pH 8.0, 150 mM NaCl, 1 mM EDTA, 0.001% LMNG (w/v), 0.025% DDM (w/v), and 0.04 % CHS (w/v)
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.90 Å
6MET Structural basis of coreceptor recognition by HIV-1 envelope spike Deposited 2018-09-07 Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain B 1–313（313 aa） Fragment：residues 1-313
Non-standard monomer：Yes (specific site not provided by mmCIF) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 7 A2G 2-acetamido-2-deoxy-alpha-D-galactopyranose × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 8；100 mM Tris-HCl, pH 8.0, 150 mM NaCl, 1 mM EDTA, 0.001% LMNG (w/v), 0.025% DDM (w/v), and 0.04 % CHS (w/v).
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.50 Å
7F1Q Cryo-EM structure of the chemokine receptor CCR5 in complex with MIP-1a and Gi Deposited 2021-06-09 Assembly 1 Insufficient information Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain R 2–319（318 aa）
Mutation：T15R,T112C,G259N No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.90 Å
7F1R Cryo-EM structure of the chemokine receptor CCR5 in complex with RANTES and Gi Deposited 2021-06-09 Assembly 1 Insufficient information Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain R 2–319（318 aa）
Mutation：F28C,G258N,E267C No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.00 Å
7F1S Cryo-EM structure of the apo chemokine receptor CCR5 in complex with Gi Deposited 2021-06-09 Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain R 2–319（318 aa）
Mutation：G163N No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.80 Å
7F1T Crystal structure of the human chemokine receptor CCR5 in complex with MIP-1a Deposited 2021-06-09 Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 2–223（222 aa）
Chain A 227–319（93 aa）
Mutation：T15C,T108C,C150Y,M156A,G255N,A376D,R417A,T427A,K446E Mutation：T15C,T108C,C150Y,M156A,G255N,A376D,R417A,T427A,K446E ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions LIPIDIC CUBIC PHASE；293 K；100mM HEPES, pH 6.0, 250mM ammonium sulfate, 30% (v/v) PEG 400, 8% (v/v) PPG 400
Resolution 2.60 Å R-free 0.271
7NJZ X-ray crystallography study of RoAb13 which binds to PIYDIN, a part of the CCR5 N terminal domain Deposited 2021-02-17 Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain C 8–13（6 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；1.85 M Ammonium sulfate
Resolution 3.20 Å R-free 0.292
7NJZ X-ray crystallography study of RoAb13 which binds to PIYDIN, a part of the CCR5 N terminal domain Deposited 2021-02-17 Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain C 8–13（6 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；1.85 M Ammonium sulfate
Resolution 3.20 Å R-free 0.292
7NW3 X-ray crystallographic study of PIYDIN, which contains the truncation determinants of binding PI and N, bound to RoAb13, a CCR5 antibody Deposited 2021-03-16 Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain A 8–13（6 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；293 K；10 mg/ml protein, 20 mM HEPES pH 7.0, 0.1 M sodium chloride, 660 uM PIYDIN peptide, 1.8 M ammonium sulfate
Resolution 3.20 Å R-free 0.293
7O7F Structural basis of the activation of the CC chemokine receptor 5 by a chemokine agonist Deposited 2021-04-13 Assembly 1 Protein heterocomplex Heteromer；Protein × 7 PDB declaration: heptameric（7） Consistent with protein count
Chain C 1–352（352 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.15 Å
9WP1 Structural insights into tyrosine sulfation of CCR5 by human tyrosylprotein sulfotransferase-1 Deposited 2025-09-08 Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric（16） Consistent with protein count
Chain L 1–6（6 aa）
Chain M 1–6（6 aa）
Chain N 1–6（6 aa）
Chain O 1–6（6 aa）
Chain P 1–6（6 aa）
Chain Q 1–6（6 aa）
Chain R 1–6（6 aa）
Chain S 1–6（6 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 3.20 Å R-free 0.323
9WP1 Structural insights into tyrosine sulfation of CCR5 by human tyrosylprotein sulfotransferase-1 Deposited 2025-09-08 Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain L 1–6（6 aa）
Chain M 1–6（6 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 3.20 Å R-free 0.323
9WP1 Structural insights into tyrosine sulfation of CCR5 by human tyrosylprotein sulfotransferase-1 Deposited 2025-09-08 Assembly 3 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain N 1–6（6 aa）
Chain O 1–6（6 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 3.20 Å R-free 0.323
9WP1 Structural insights into tyrosine sulfation of CCR5 by human tyrosylprotein sulfotransferase-1 Deposited 2025-09-08 Assembly 4 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain P 1–6（6 aa）
Chain Q 1–6（6 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 3.20 Å R-free 0.323
9WP1 Structural insights into tyrosine sulfation of CCR5 by human tyrosylprotein sulfotransferase-1 Deposited 2025-09-08 Assembly 5 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain R 1–6（6 aa）
Chain S 1–6（6 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 3.20 Å R-free 0.323

This page presents structural evidence recorded in PDB/mmCIF.“No recorded non-water small molecule” does not prove that the experimental sample was ligand-free; experimental conditions belong to the PDB experiment, while ligands and copy counts are shown for each biological assembly.