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Crystal structure of KPC-2 with compound 6
Analyse Crystal structure of KPC-2 with compound 6 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6MNP
- Type
- protein
- Length
- 266 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.202
- Source
- Klebsiella pneumoniae
- Molecule
- Carbapenem-hydrolyzing beta-lactamase KPC
- EC
- 3.5.2.6
- UniProt
- Q9F663
- Ligands
- 1CE
Structure
x-ray diffraction · resolution 2.202 · 1 distinct chain · 43% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Carbapenem-hydrolyzing beta-lactamase KPC (EC 3.5.2.6) | protein | 266 | 43% helix, 17% strand | Q9F663 |
Ligands and binding sites
- 1CE · 3-(1H-tetrazol-5-ylmethyl)-5,6,7,8-tetrahydro[1]benzothieno[2,3-d]pyrimidin-4(3H)-one · ligand · 3 copies · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
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 Q9F663
- Elsewhere: RCSB PDB 6MNP · PDBe 6MNP · UniProt Q9F663
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