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Crystal structure of the bifunctional mannitol-1-phosphate DEHYDROGENASE/PHOSPHATASE mtld from acinetobacter baumannii
Analyse Crystal structure of the bifunctional mannitol-1-phosphate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7OCN
- Type
- protein
- Length
- 1,369 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- D0C7J2
- Ligands
- MG, SO4, CL, BR
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 690 | — | D0C7J2 |
| B | — | protein | 679 | — | D0C7J2 |
Ligands and binding sites
- MG · Magnesium ion · metal · 3 copies · chains A, B
- SO4 · Sulfate ion · ion · 4 copies · chains A, B
- CL · Chloride ion · ion · 4 copies · chains A, B
- BR · Bromide ion · ion · chains A
- EDO · 1,2-ethanediol · additive · 2 copies · chains A, B
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7OCN · Crystal structure of the bifunctional mannitol-1-phosphate dehydrogenase/phosphatase MtlD… · 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 D0C7J2
- Elsewhere: RCSB PDB 7OCN · PDBe 7OCN · UniProt D0C7J2
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