MolNFT v1 · #136379 · protein
Crystal structure of proline utilization a (puta) from bdellovibrio bacteriovorus inactivated by N-propargylglycine
5UR2: “Crystal structure of proline utilization a (puta) from bdellovibrio bacteriovorus inactivated by…”. X-ray diffraction, 1 ligand (P5F). MolNFT v1 #136379 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5UR2
- Type
- protein
- Length
- 3,832 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q6MNK1
- Ligands
- P5F
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 956 | — | Q6MNK1 |
| B | — | protein | 959 | — | Q6MNK1 |
| C | — | protein | 958 | — | Q6MNK1 |
| D | — | protein | 959 | — | Q6MNK1 |
Ligands and binding sites
- P5F · N-propargylglycine-modified flavin adenine dinucleotide · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5UR2 · Crystal structure of proline utilization A (PutA) from Bdellovibrio bacteriovorus… · 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 Q6MNK1
- Elsewhere: RCSB PDB 5UR2 · PDBe 5UR2 · UniProt Q6MNK1
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