Research workbench
Crystal structure of the apomolybdo-narghi
Analyse Crystal structure of the apomolybdo-narghi in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1SIW
- Type
- protein
- Length
- 1,967 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P09152, P11349, P11350
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 1240 | — | P09152 |
| B | — | protein | 508 | — | P11349 |
| C | — | protein | 219 | — | P11350 |
Compared structures
- 1SIW · Crystal structure of the apomolybdo-NarGHI · the same entry in another collection · chain A against A, TM-score 1.00
- P09152 · AlphaFold monomer V2.0 prediction for respiratory nitrate reductase 1 alpha chain (P09152) · a predicted model of the same protein · chain A against A, TM-score 1.00
- P11349 · AlphaFold monomer V2.0 prediction for respiratory nitrate reductase 1 beta chain (P11349) · a predicted model of the same protein · chain B against A, TM-score 1.00
- P11350 · AlphaFold monomer V2.0 prediction for respiratory nitrate reductase 1 gamma chain (P11350) · a predicted model of the same protein · chain C 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 P09152
- Every structure of UniProt P11349
- Every structure of UniProt P11350
- Elsewhere: RCSB PDB 1SIW · PDBe 1SIW · UniProt P09152 · UniProt P11349 · UniProt P11350
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