MolNFT v1 · #144138 · protein + DNA
Lysyl-adenylate form of human ligiv catalytic domain with bound DNA substrate in open conformation
6BKF: “Lysyl-adenylate form of human ligiv catalytic domain with bound DNA substrate in open conformation”. X-ray diffraction, 1 ligand (AMP). MolNFT v1 #144138 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6BKF
- Type
- protein + DNA
- Length
- 598 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P49917
- Ligands
- AMP
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 562 | — | P49917 |
| P | — | dna | 11 | — | — |
| T | — | dna | 18 | — | — |
| D | — | dna | 7 | — | — |
Ligands and binding sites
- AMP · Adenosine monophosphate · ligand · chains A, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6BKF · Lysyl-adenylate form of human LigIV catalytic domain with bound DNA substrate in open… · the same entry in another collection · chain A against A, TM-score 1.00
- P49917 · AlphaFold monomer V2.0 prediction for DNA ligase 4 (P49917) · a predicted model of the same protein · chain A against A, TM-score 0.77
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 P49917
- Elsewhere: RCSB PDB 6BKF · PDBe 6BKF · UniProt P49917
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