MolNFT v1 · #162822 · protein
Inter-dimeric interface controls function and stability of S- methionine adenosyltransferase from U. urealiticum
6RK7: “Inter-dimeric interface controls function and stability of S- methionine adenosyltransferase from U.…”. X-ray diffraction, 1 ligand (CL). MolNFT v1 #162822 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6RK7
- Type
- protein
- Length
- 2,257 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- B2NE58
- Ligands
- CL
Structure
x-ray diffraction · 5 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 376 | — | B2NE58 |
| B, F | — | protein | 376 | — | B2NE58 |
| E | — | protein | 377 | — | B2NE58 |
| G | — | protein | 377 | — | B2NE58 |
| H | — | protein | 375 | — | B2NE58 |
Ligands and binding sites
- CL · Chloride ion · ion · 6 copies · chains A, B, E, F, G, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6RK7 · Inter-dimeric interface controls function and stability of S-methionine… · the same entry in another collection · chain E against E, TM-score 0.99
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 B2NE58
- Elsewhere: RCSB PDB 6RK7 · PDBe 6RK7 · UniProt B2NE58
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