Research workbench
6ALPHA-(HYDROXYPROPYL)PENICILLANATE acylated on nmc-a beta- lactamase from enterobacter cloacae
Analyse 6ALPHA-(HYDROXYPROPYL)PENICILLANATE acylated on nmc-a beta- lactamase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1BUL
- Type
- protein
- Length
- 265 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nmc-a beta-lactamase
- EC
- 3.5.2.6
- UniProt
- P52663
- Ligands
- AP3
- Pockets
- 1 · best druggability 0.27
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nmc-a beta-lactamase (EC 3.5.2.6) | protein | 265 | 42% helix, 17% strand | P52663 |
Ligands and binding sites
- AP3 · 2-(1-carboxy-2-hydroxy-2-methyl-propyl)-5,5-dimethyl-thiazolidine-4-carboxylic acid · ligand · chains A
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 56 | 0.27 | 0.74 | 18 | AP3 |
Modifications
Observed in the structure: 1 covalent, 1 disulfide (covalent ligand, disulfide).
Compared structures
- 1BUL · 6ALPHA-(HYDROXYPROPYL)PENICILLANATE acylated on nmc-a beta-lactamase from enterobacter… · the same entry in another collection · chain A against A, TM-score 1.00
- P52663 · AlphaFold monomer V2.0 prediction for imipenem-hydrolyzing beta- lactamase (P52663) · a predicted model of the same protein · 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 P52663
- Elsewhere: RCSB PDB 1BUL · PDBe 1BUL · UniProt P52663
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