SAXSdb — 5cmd

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

C-C motif chemokine 5

Homo sapiens

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 homooligomer Homooligomer Protein × 6 PDB declaration: hexameric（6） Consistent with protein copy count	Chain A； UniProt 27–91 Chain B； UniProt 27–91 Chain C； UniProt 27–91 Chain D； UniProt 27–91 Chain E； UniProt 27–91 Chain F； UniProt 27–91	Fragment：unp residues 27-91	SO4 SULFATE ION × 11	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7.5；303.15 K；0.1 M Tris, 1.8 M Ammonium sulfate	Resolution 3.09 Å R-free 0.258

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 5CMD	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1B3A TOTAL CHEMICAL SYNTHESIS AND HIGH-RESOLUTION CRYSTAL STRUCTURE OF THE POTENT ANTI-HIV PROTEIN AOP-RANTES Deposited 1998-12-07	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 10–76（67 aa）	Not recorded	SO4 SULFATE ION × 3 AOP PENTYLOXYAMINO-ACETALDEHYDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.6；pH 4.6	Resolution 1.60 Å R-free 0.241
1B3A TOTAL CHEMICAL SYNTHESIS AND HIGH-RESOLUTION CRYSTAL STRUCTURE OF THE POTENT ANTI-HIV PROTEIN AOP-RANTES Deposited 1998-12-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 10–76（67 aa）	Not recorded	SO4 SULFATE ION × 1 AOP PENTYLOXYAMINO-ACETALDEHYDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.6；pH 4.6	Resolution 1.60 Å R-free 0.241
1EQT MET-RANTES Deposited 2000-04-06	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 25–91（67 aa） Chain B 25–91（67 aa）	Not recorded	SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；295 K；PEG 35000, ammonium sulfate, sodium succinate, MES, sodium acetate, ethanol, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 295.0K	Resolution 1.60 Å R-free 0.251
1HRJ HUMAN RANTES, NMR, 13 STRUCTURES Deposited 1995-08-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 24–91（68 aa） Chain B 24–91（68 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
1RTN PROTON NMR ASSIGNMENTS AND SOLUTION CONFORMATION OF RANTES, A CHEMOKINE OF THE CC TYPE Deposited 1995-02-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 24–91（68 aa） Chain B 24–91（68 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
1RTO PROTON NMR ASSIGNMENTS AND SOLUTION CONFORMATION OF RANTES, A CHEMOKINE OF THE CC TYPE Deposited 1995-02-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 24–91（68 aa） Chain B 24–91（68 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
1U4L human RANTES complexed to heparin-derived disaccharide I-S Deposited 2004-07-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 24–91（68 aa） Chain B 24–91（68 aa）	Not recorded	ACY ACETIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；293 K；15% (w/v) PEG 400, 100mM acetate buffer, 1mM Heparin Disaccharide I-S, 10% (w/v) glycerol, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.00 Å R-free 0.255
1U4M human RANTES complexed to heparin-derived disaccharide III-S Deposited 2004-07-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 24–91（68 aa） Chain B 24–91（68 aa）	Not recorded	ACY ACETIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；293 K；15% (w/v) PEG 400, 100mM acetate buffer, 1mM Heparin Disaccharide III-S, 10% (w/v) glycerol, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.00 Å R-free 0.252
1U4P Crystal Structure of human RANTES mutant K45E Deposited 2004-07-26	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 24–91（68 aa） Chain B 24–91（68 aa）	Mutation：K45E Mutation：K45E	ACY ACETIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；293 K；20% PEG 400, 100mM acetate buffer, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 1.70 Å R-free 0.254
1U4R Crystal Structure of human RANTES mutant 44-AANA-47 Deposited 2004-07-26	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 24–91（68 aa） Chain B 24–91（68 aa）	Mutation：R44A, K45A, R47A Mutation：R44A, K45A, R47A	SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；293 K；25% PEG 400, 100mM acetate buffer, 200mM (NH4)2SO4, 10% (v/v) glycerol, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.20 Å R-free 0.306
1U4R Crystal Structure of human RANTES mutant 44-AANA-47 Deposited 2004-07-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 24–91（68 aa） Chain D 24–91（68 aa）	Mutation：R44A, K45A, R47A Mutation：R44A, K45A, R47A	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；293 K；25% PEG 400, 100mM acetate buffer, 200mM (NH4)2SO4, 10% (v/v) glycerol, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.20 Å R-free 0.306
2L9H Oligomeric Structure of the Chemokine CCL5/RANTES from NMR, MS, and SAXS Data Deposited 2011-02-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 24–91（68 aa） Chain B 24–91（68 aa） Chain C 24–91（68 aa） Chain D 24–91（68 aa）	Not recorded	No recorded non-water small molecule	Experimental method not declared NMR measurement conditions pH 4.4；297 K；Ionic strength (raw mmCIF value) 0.05；Pressure ambient NMR sample composition 1 mM [U-100% 15N] ccl5, 50 mM sodium acetate, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 1 mM [U-100% 15N] ccl5, 50 mM sodium acetate, 5 % polyacrylamide, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
2VXW Structural and Functional Studies of the Potent Anti-HIV Chemokine Variant P2-RANTES Deposited 2008-07-12	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 33–91（59 aa） Fragment：CHEMOKINE, RESIDUES 33-91 Chain B 33–91（59 aa） Fragment：CHEMOKINE, RESIDUES 33-91 Chain C 33–91（59 aa） Fragment：CHEMOKINE, RESIDUES 33-91 Chain D 33–91（59 aa） Fragment：CHEMOKINE, RESIDUES 33-91	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.5；pH 5.5	Resolution 1.70 Å R-free 0.248
5COY Crystal structure of CC chemokine 5 (CCL5) Deposited 2015-07-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 27–91（65 aa） Chain B 27–91（65 aa）	Not recorded	PO4 PHOSPHATE ION × 2 PEG DI(HYDROXYETHYL)ETHER × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291.15 K；0.2 M Potassium phosphate monobasic, 20% w/v Polyethylene glycol 3,350	Resolution 1.44 Å R-free 0.192
5DNF Crystal structure of CC chemokine 5 (CCL5) oligomer in complex with heparin Deposited 2015-09-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 9 PDB declaration: nonameric	Chain A 27–91（65 aa） Fragment：UNP residues 27-91 Chain B 27–91（65 aa） Fragment：UNP residues 27-91 Chain C 27–91（65 aa） Fragment：UNP residues 27-91 Chain D 27–91（65 aa） Fragment：UNP residues 27-91 Chain E 27–91（65 aa） Fragment：UNP residues 27-91 Chain F 27–91（65 aa） Fragment：UNP residues 27-91 Chain G 27–91（65 aa） Fragment：UNP residues 27-91 Chain H 27–91（65 aa） Fragment：UNP residues 27-91 Chain I 27–91（65 aa） Fragment：UNP residues 27-91	Mutation：S4TNR Mutation：S4TNR Mutation：S4TNR Mutation：S4TNR Mutation：S4TNR Mutation：S4TNR Mutation：S4TNR Mutation：S4TNR Mutation：S4TNR	GLA alpha-D-galactopyranose × 6 BGC beta-D-glucopyranose × 5 SO4 SULFATE ION × 5 CL CHLORIDE ION × 20 TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；303.15 K；0.1M Tris, pH 7.5; 1.8 M (NH4)2SO4	Resolution 2.55 Å R-free 0.234
5L2U Oligomer crystal structure of CC chemokine 5 (CCL5) Deposited 2016-08-02	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 27–91（65 aa） Fragment：UNP residues 27-91 Chain B 27–91（65 aa） Fragment：UNP residues 27-91 Chain C 27–91（65 aa） Fragment：UNP residues 27-91 Chain D 27–91（65 aa） Fragment：UNP residues 27-91 Chain E 27–91（65 aa） Fragment：UNP residues 27-91 Chain F 27–91（65 aa） Fragment：UNP residues 27-91	Not recorded	EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 2 CL CHLORIDE ION × 2 GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.8；303.15 K；0.1 HEPES, 300 mM NaCl, 3.5% 2-propanol	Resolution 2.28 Å R-free 0.209
5L2U Oligomer crystal structure of CC chemokine 5 (CCL5) Deposited 2016-08-02	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain G 27–91（65 aa） Fragment：UNP residues 27-91 Chain H 27–91（65 aa） Fragment：UNP residues 27-91 Chain I 27–91（65 aa） Fragment：UNP residues 27-91	Not recorded	EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.8；303.15 K；0.1 HEPES, 300 mM NaCl, 3.5% 2-propanol	Resolution 2.28 Å R-free 0.209
5UIW Crystal Structure of CC Chemokine Receptor 5 (CCR5) in complex with high potency HIV entry inhibitor 5P7-CCL5 Deposited 2017-01-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 33–91（59 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	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
6AEZ Crystal structure of human CCL5 trimer Deposited 2018-08-07	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 24–91（68 aa） Chain B 24–91（68 aa） Chain C 24–91（68 aa）	Mutation：E67S Mutation：E67S	SO4 SULFATE ION × 12	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；283 K；0.2M ammonium sulfate, 0.1M BIS-TRIS pH 5, 16% (w/v) polyethylene glycol 3350	Resolution 1.63 Å R-free 0.228
6C6D 20mer crystal structure of CC chemokine 5 (CCL5) Deposited 2018-01-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 20 PDB declaration: eicosameric	Chain A 27–91（65 aa） Fragment：UNP Residues 27-91 Chain B 27–91（65 aa） Fragment：UNP Residues 27-91 Chain C 27–91（65 aa） Fragment：UNP Residues 27-91 Chain D 27–91（65 aa） Fragment：UNP Residues 27-91 Chain E 27–91（65 aa） Fragment：UNP Residues 27-91 Chain F 27–91（65 aa） Fragment：UNP Residues 27-91 Chain G 27–91（65 aa） Fragment：UNP Residues 27-91 Chain H 27–91（65 aa） Fragment：UNP Residues 27-91 Chain I 27–91（65 aa） Fragment：UNP Residues 27-91 Chain J 27–91（65 aa） Fragment：UNP Residues 27-91 Chain K 27–91（65 aa） Fragment：UNP Residues 27-91 Chain L 27–91（65 aa） Fragment：UNP Residues 27-91 Chain M 27–91（65 aa） Fragment：UNP Residues 27-91 Chain N 27–91（65 aa） Fragment：UNP Residues 27-91 Chain O 27–91（65 aa） Fragment：UNP Residues 27-91 Chain P 27–91（65 aa） Fragment：UNP Residues 27-91 Chain Q 27–91（65 aa） Fragment：UNP Residues 27-91 Chain R 27–91（65 aa） Fragment：UNP Residues 27-91 Chain S 27–91（65 aa） Fragment：UNP Residues 27-91 Chain T 27–91（65 aa） Fragment：UNP Residues 27-91	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；303.15 K；10% (v/v) 2-propanol, 0.1M HEPES pH 7.5, 0.2M NaCl	Resolution 5.50 Å R-free 0.286
6FGP NMR solution structure of monomeric CCL5 in complex with a doubly-sulfated N-terminal segment of CCR5 Deposited 2018-01-11	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 24–91（68 aa）	Mutation：i	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
6LOG Crystal structure of human CCL5-12AAA14 mutant Deposited 2020-01-05	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 24–91（68 aa）	Mutation：F12A, Y14A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.9；283 K；0.2M Magnesium acetate tetrahydrate pH 7.9, 20% PEG 3350	Resolution 2.55 Å R-free 0.249
6STK Crystal structure of the CC-chemokine 5 (CCL5) E66S mutation Deposited 2019-09-10	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 24–91（68 aa） Chain B 24–91（68 aa）	Mutation：E66S Mutation：E66S	ACT ACETATE ION × 1 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；15% glycerol, 25.5% PEG 4000, 85mM acetate buffer pH 4.6, 0.17 M ammonium acetate	Resolution 1.52 Å R-free 0.203
7F1R Cryo-EM structure of the chemokine receptor CCR5 in complex with RANTES and Gi Deposited 2021-06-09	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 × 4 PDB declaration: tetrameric	Chain R 24–91（68 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
7O7F Structural basis of the activation of the CC chemokine receptor 5 by a chemokine agonist Deposited 2021-04-13	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 × 7 PDB declaration: heptameric	Chain I 23–91（69 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.15 Å

22 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	CCL5_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–65； UniProt 27–91 Author chain B； PDBConstruct 1–65； UniProt 27–91 Author chain C； PDBConstruct 1–65； UniProt 27–91 Author chain D； PDBConstruct 1–65； UniProt 27–91 Author chain E； PDBConstruct 1–65； UniProt 27–91 Author chain F； PDBConstruct 1–65； UniProt 27–91

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	5cmd
Deposition date deposition_date	2015-07-16
Structure title title	Oligomer crystal structure of CC chemokine 5 (CCL5)
Keywords keywords	CC chemokine, high oligomer, CYTOKINE; CYTOKINE
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	25.26 Å
Radius of gyration Rg (electron density) rg_electron	24.09 Å
Forward intensity I(0) i0	37666400.00
Molecular weight molecular_weight	45397.0 kDa
Excluded volume excluded_volume	56053 Å³
Envelope volume envelope_volume	74804 Å³
Hydration-shell volume shell_volume	25983 Å³
Envelope diameter envelope_diameter	82.2 Å
Shell Rg shell_rg	31.26 Å
Envelope Rg envelope_rg	23.84 Å
Shape Rg shape_rg	24.05 Å
Total Rg total_rg	25.08 Å
Total atoms total_atoms	3163
Residues n_residues	383
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	79.5 Å
Rg (real space) rg_real	25.14 Å
Rg uncertainty (real space) rg_real_error	0.50 Å
I(0) (real space) i0_real	3.7670e+07
I(0) uncertainty (real space) i0_real_error	5.5190e+05
Rg (reciprocal space) rg_reciprocal	25.18 Å
I(0) (reciprocal space) i0_reciprocal	37670000.0000
Solution quality estimate total_estimate	0.9074
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	31.6 Å
Skewness Skewness skewness	0.118
Kurtosis Kurtosis kurtosis	-0.580
Angular range angular_range	— – 0.3150 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	6040000.0000
Real-space data points n_real_points	64
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: 1.000; Smooth: 0.996

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

Domain ID domain_id	d5cmda_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.9 — IL8-like
Superfamily Superfamily superfamily	d.9.1 — Interleukin 8-like chemokines
Family Family family	d.9.1.1 — Interleukin 8-like chemokines

Domain ID domain_id	d5cmdb_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.9 — IL8-like
Superfamily Superfamily superfamily	d.9.1 — Interleukin 8-like chemokines
Family Family family	d.9.1.1 — Interleukin 8-like chemokines

Domain ID domain_id	d5cmdc_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.9 — IL8-like
Superfamily Superfamily superfamily	d.9.1 — Interleukin 8-like chemokines
Family Family family	d.9.1.1 — Interleukin 8-like chemokines

Domain ID domain_id	d5cmdd_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.9 — IL8-like
Superfamily Superfamily superfamily	d.9.1 — Interleukin 8-like chemokines
Family Family family	d.9.1.1 — Interleukin 8-like chemokines

Domain ID domain_id	d5cmde_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.9 — IL8-like
Superfamily Superfamily superfamily	d.9.1 — Interleukin 8-like chemokines
Family Family family	d.9.1.1 — Interleukin 8-like chemokines

Domain ID domain_id	d5cmdf_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.9 — IL8-like
Superfamily Superfamily superfamily	d.9.1 — Interleukin 8-like chemokines
Family Family family	d.9.1.1 — Interleukin 8-like chemokines

CATH v4.4 (6 domains)

Domain ID domain_id	5cmdA00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	40 —

Domain ID domain_id	5cmdB00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	40 —

Domain ID domain_id	5cmdC00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	40 —

Domain ID domain_id	5cmdD00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	40 —

Domain ID domain_id	5cmdE00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	40 —

Domain ID domain_id	5cmdF00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	40 —

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8. Citations (1)

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Unit-cell length a length_a	124.720 Å
Unit-cell length b length_b	124.720 Å
Unit-cell length c length_c	127.050 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	36

Space group space_group	P 62
Space-group number int_tables_number	171
Crystal system crystal_system	—

Resolution resolution	3.086 Å
Low-resolution limit resolution_low	40.824 Å
R factor r_factor	0.2173
R_work r_work	0.2130
R_free r_free	0.2577

Description description	C-C motif chemokine 5
Molecular weight formula_weight	7514.6 kDa
Source method src_method	man
Copy count entity_count	6

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F
Atom count atom_count	3163

Oligomer crystal structure of CC chemokine 5 (CCL5)

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

C-C motif chemokine 5

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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 non-polymer

7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

CATH v4.4 (6 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

来源生物 organism	Homo sapiens
通用名 common_name	Human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

Description description	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	11

fit	/app/data/saxs_computation/cm/5cmd/5cmd.fit
pddf	/app/data/pr_computation/cm/5cmd/5cmd.pr.out
profile	/app/data/saxs_computation/cm/5cmd/5cmd.dat