Research workbench
Crystal structure of the human chemokine receptor CCR5 in complex with mip-1A
Analyse Crystal structure of the human chemokine receptor CCR5 in complex with mip-1A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7F1T
- Type
- protein
- Length
- 423 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P10147, P51681, P00268
- Ligands
- ZN
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 423 | — | P10147, P51681, P00268 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7F1T · Crystal structure of the human chemokine receptor CCR5 in complex with MIP-1a · the same entry in another collection · chain A against A, TM-score 1.00
- P51681 · AlphaFold monomer V2.0 prediction for C-C chemokine receptor type 5 (P51681) · a predicted model of the same protein · chain A against A, TM-score 0.69
- P10147 · AlphaFold monomer V2.0 prediction for C-C motif chemokine 3 (P10147) · a predicted model of the same protein · chain A against A, TM-score 0.15
- P00268 · AlphaFold monomer V2.0 prediction for rubredoxin (P00268) · a predicted model of the same protein · chain A against A, TM-score 0.12
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P10147
- Every structure of UniProt P51681
- Every structure of UniProt P00268
- Elsewhere: RCSB PDB 7F1T · PDBe 7F1T · UniProt P10147 · UniProt P51681 · UniProt P00268
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