Research workbench
Crystal structure of dihydrodipicolinate reductase from acinetobacter baumannii
Analyse Crystal structure of dihydrodipicolinate reductase from acinetobacter baumannii in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 8D57
- Type
- protein
- Length
- 1,602 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A0D5YCZ0
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E, F | — | protein | 267 | — | A0A0D5YCZ0 |
| B | — | protein | 268 | — | A0A0D5YCZ0 |
| D | — | protein | 266 | — | A0A0D5YCZ0 |
Ligands and binding sites
- CIT · Citric acid · additive · 6 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 8D57 · Crystal Structure of dihydrodipicolinate reductase from Acinetobacter baumannii · the same entry in another collection · 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 A0A0D5YCZ0
- Elsewhere: RCSB PDB 8D57 · PDBe 8D57 · UniProt A0A0D5YCZ0
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