Research workbench
Crystal structure of cmy-136 class C beta-lactamase
Analyse Crystal structure of cmy-136 class C beta-lactamase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6G9T
- Type
- protein
- Length
- 718 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- G3F7G9
- Ligands
- PO4
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 359 | — | G3F7G9 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 5 copies · chains A, B
- IPA · Isopropyl alcohol · additive · 5 copies · chains A, B
- GOL · Glycerol · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6G9T · CRYSTAL STRUCTURE OF CMY-136 class C BETA-LACTAMASE · 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 G3F7G9
- Elsewhere: RCSB PDB 6G9T · PDBe 6G9T · UniProt G3F7G9
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