Research workbench
Crystal structure of human D-amino acid oxidase mutant (P219L) complexed with benzoate
Analyse Crystal structure of human D-amino acid oxidase mutant (P219L) complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6KBP
- Type
- protein
- Length
- 1,347 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P14920
- Ligands
- FAD, BEZ
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 336 | — | P14920 |
| B | — | protein | 336 | — | P14920 |
| C | — | protein | 338 | — | P14920 |
| D | — | protein | 337 | — | P14920 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 4 copies · chains A, B, C, D
- BEZ · Benzoic acid · ligand · 4 copies · chains A, B, C, D
- ACT · Acetate ion · additive · 2 copies · chains B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6KBP · Crystal structure of human D-amino acid oxidase mutant (P219L) complexed with benzoate · the same entry in another collection · chain D against D, TM-score 1.00
- P14920 · AlphaFold monomer V2.0 prediction for D-amino-acid oxidase (P14920) · 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 P14920
- Elsewhere: RCSB PDB 6KBP · PDBe 6KBP · UniProt P14920
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