MolNFT v1 · #138528 · protein + DNA
Structure of the 10S (+)-trans-bp-dg modified REV1 ternary complex
5WM1: “Structure of the 10S (+)-trans-bp-dg modified REV1 ternary complex”. X-ray diffraction, 2 ligands (DCP, MG). MolNFT v1 #138528 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5WM1
- Type
- protein + DNA
- Length
- 462 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P12689
- Ligands
- DCP, MG
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| P | — | dna | 12 | — | — |
| T | — | dna | 17 | — | — |
| A | — | protein | 433 | — | P12689 |
Ligands and binding sites
- DCP · 2'-deoxycytidine-5'-triphosphate · ligand · chains P, A
- MG · Magnesium ion · metal · 4 copies · chains P, A
- EDO · 1,2-ethanediol · additive · 8 copies · chains T, A
- GOL · Glycerol · additive · 5 copies · chains A, T
- PEG · Di(hydroxyethyl)ether · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5WM1 · Structure of the 10S (+)-trans-BP-dG modified Rev1 ternary complex · the same entry in another collection · chain P against P, TM-score 1.00
- P12689 · AlphaFold monomer V2.0 prediction for DNA repair protein REV1 (P12689) · a predicted model of the same protein · chain A against A, TM-score 1.00
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 P12689
- Elsewhere: RCSB PDB 5WM1 · PDBe 5WM1 · UniProt P12689
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