MolNFT v1 · #187692 · protein
Structure of the E. COLI puta proline dehydrogenase domain (residues 86-630) complexed with (2S)-oxetane-2-carboxylic acid
7SQN: “Structure of the E. COLI puta proline dehydrogenase domain (residues 86-630) complexed with…”. X-ray diffraction, 2 ligands (FAD, A8G). MolNFT v1 #187692 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7SQN
- Type
- protein
- Length
- 503 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A383H020
- Ligands
- FAD, A8G
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 503 | — | A0A383H020 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · chains A
- A8G · (2S)-oxetane-2-carboxylic acid · ligand · chains A
- PGE · Triethylene glycol · additive · chains A
- 1PE · Pentaethylene glycol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7SQN · Structure of the E. coli PutA proline dehydrogenase domain (residues 86-630) complexed… · 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 A0A383H020
- Elsewhere: RCSB PDB 7SQN · PDBe 7SQN · UniProt A0A383H020
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