MolNFT v1 · #184401 · protein
Crystal structure of complement C5 in complex with chemically synthesized K92 knob domain.
7OP0: “Crystal structure of complement C5 in complex with chemically synthesized K92 knob domain.”. X-ray diffraction, 1 ligand (NAG). MolNFT v1 #184401 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7OP0
- Type
- protein
- Length
- 1,654 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P01031
- Ligands
- NAG
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 972 | — | P01031 |
| B | — | protein | 647 | — | P01031 |
| C | — | protein | 35 | — | — |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
- EDO · 1,2-ethanediol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7OP0 · Crystal structure of complement C5 in complex with chemically synthesized K92 knob domain. · the same entry in another collection · chain A against A, TM-score 1.00
- P01031 · AlphaFold monomer V2.0 prediction for complement C5 (P01031) · a predicted model of the same protein · chain B against A, TM-score 0.97
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 P01031
- Elsewhere: RCSB PDB 7OP0 · PDBe 7OP0 · UniProt P01031
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