MolNFT v1 · #158404 · protein
Crystallographic capture of quinolinate synthase (nada) from pyrococcus horikoshii in its substrates and product-bound states
6NSU: “Crystallographic capture of quinolinate synthase (nada) from pyrococcus horikoshii in its substrates and…”. X-ray diffraction, 1 ligand (SF4). MolNFT v1 #158404 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6NSU
- Type
- protein
- Length
- 299 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O57767
- Ligands
- SF4
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 299 | — | O57767 |
Ligands and binding sites
- SF4 · Iron/sulfur cluster · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6NSU · Crystallographic Capture of Quinolinate Synthase (NadA) from Pyrococcus horikoshii in its… · the same entry in another collection · chain A against A, TM-score 1.00
- O57767 · AlphaFold monomer V2.0 prediction for quinolinate synthase a (O57767) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 O57767
- Elsewhere: RCSB PDB 6NSU · PDBe 6NSU · UniProt O57767
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