MolNFT v1 · #167353 · protein
Observing a ring-cleaving dioxygenase in action through a crystalline lens - a substrate monodentately bound structure
6VI6: “Observing a ring-cleaving dioxygenase in action through a crystalline lens - a substrate monodentately bound…”. X-ray diffraction, 2 ligands (3HA, FE2). MolNFT v1 #167353 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6VI6
- Type
- protein
- Length
- 174 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q1LCS4
- Ligands
- 3HA, FE2
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 174 | — | Q1LCS4 |
Ligands and binding sites
- 3HA · 3-hydroxyanthranilic acid · ligand · chains A
- FE2 · Fe (II) ion · metal · 2 copies · chains A
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6VI6 · Observing a ring-cleaving dioxygenase in action through a crystalline lens - a substrate… · the same entry in another collection · chain A against A, TM-score 1.00
- Q1LCS4 · AlphaFold monomer V2.0 prediction for 3-hydroxyanthranilate 3,4-dioxygenase (Q1LCS4) · a predicted model of the same protein · chain A against A, 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 Q1LCS4
- Elsewhere: RCSB PDB 6VI6 · PDBe 6VI6 · UniProt Q1LCS4
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