MolNFT v1 · #160427 · protein
Adenylate kinase from methanococcus igneus - apo form
6PK5: “Adenylate kinase from methanococcus igneus - apo form”. X-ray diffraction, 1 ligand (CL). MolNFT v1 #160427 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6PK5
- Type
- protein
- Length
- 1,137 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P43408
- Ligands
- CL
Structure
x-ray diffraction · 6 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 188 | — | P43408 |
| B | — | protein | 189 | — | P43408 |
| C | — | protein | 190 | — | P43408 |
| D | — | protein | 191 | — | P43408 |
| E | — | protein | 189 | — | P43408 |
| F | — | protein | 190 | — | P43408 |
Ligands and binding sites
- CL · Chloride ion · ion · 15 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
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 P43408
- Elsewhere: RCSB PDB 6PK5 · PDBe 6PK5 · UniProt P43408
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