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Crystal structure of a beta-lactamase-like protein from brucella melitensis bound to AMP
Analyse Crystal structure of a beta-lactamase-like protein from brucella melitensis… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3PY5
- Type
- protein
- Length
- 270 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-lactamase-like
- UniProt
- Q2YQ74
- Ligands
- AMP, MN, K
Structure
x-ray diffraction · 1 distinct chain · 24% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-lactamase-like | protein | 270 | 24% helix, 31% strand | Q2YQ74 |
Ligands and binding sites
- AMP · Adenosine monophosphate · ligand · chains A
- MN · Manganese (II) ion · metal · 2 copies · chains A
- K · Potassium ion · metal · chains A
- TLA · L(+)-tartaric acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 3PY5 · Crystal structure of a beta-lactamase-like protein from brucella melitensis bound to AMP · 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 Q2YQ74
- Elsewhere: RCSB PDB 3PY5 · PDBe 3PY5 · UniProt Q2YQ74
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