Research workbench
Crystal structure of N-ethylmaleimide reductase from klebsiella pneumoniae
Analyse Crystal structure of N-ethylmaleimide reductase from klebsiella pneumoniae in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7TMB
- Type
- protein
- Length
- 2,164 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A0H3GQS4
- Ligands
- FMN, NA
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D, E | — | protein | 362 | — | A0A0H3GQS4 |
| B, F | — | protein | 359 | — | A0A0H3GQS4 |
| C | — | protein | 360 | — | A0A0H3GQS4 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · 6 copies · chains A, B, C, D, E, F
- NA · Sodium ion · metal · 6 copies
- PG4 · Tetraethylene glycol · additive · 12 copies · chains A, C, F, B, D, E
- FLC · Citrate anion · additive · 6 copies · chains B, D, C, F, A, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7TMB · Crystal Structure of N-ethylmaleimide reductase from Klebsiella pneumoniae · 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 A0A0H3GQS4
- Elsewhere: RCSB PDB 7TMB · PDBe 7TMB · UniProt A0A0H3GQS4
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