Research workbench
Crystal structure of metallo-beta-lactamase from thermotoga maritima
Analyse Crystal structure of metallo-beta-lactamase from thermotoga maritima in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3X30
- Type
- protein
- Length
- 227 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- UPF0173 metal-dependent hydrolase TM_1162
- UniProt
- Q9X0P5
- Ligands
- MN, NI
Structure
x-ray diffraction · 1 distinct chain · 25% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | UPF0173 metal-dependent hydrolase TM_1162 | protein | 227 | 25% helix, 31% strand | Q9X0P5 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 8 modified (engineered).
Compared structures
- 3X30 · Crystal structure of metallo-beta-lactamase from Thermotoga maritima · the same entry in another collection · chain A against A, TM-score 1.00
- Q9X0P5 · AlphaFold monomer V2.0 prediction for UPF0173 metal-dependent hydrolase TM_1162 (Q9X0P5) · 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 Q9X0P5
- Elsewhere: RCSB PDB 3X30 · PDBe 3X30 · UniProt Q9X0P5
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