Research workbench
Crystal structure of ctx-M-14 in complex with temocillin
Analyse Crystal structure of ctx-M-14 in complex with temocillin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6UNB
- Type
- protein
- Length
- 523 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A2S1PK93
- Ligands
- TJ7, PO4
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 263 | — | A0A2S1PK93 |
| B | — | protein | 260 | — | A0A2S1PK93 |
Ligands and binding sites
- TJ7 · (2R,4S)-2-[(1S)-1-{[(2R)-2-carboxy-2-(thiophen-3-yl) acetyl]amino}-1-methoxy-2-oxoethyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid · ligand · 2 copies · chains A, B
- PO4 · Phosphate ion · ion · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6UNB · Crystal structure of CTX-M-14 in complex with temocillin · 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 A0A2S1PK93
- Elsewhere: RCSB PDB 6UNB · PDBe 6UNB · UniProt A0A2S1PK93
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