MolNFT v1 · #164020 · protein
Oxa-655_MEM. structural insights into the enhanced carbapenemase efficiency of oxa-655 compared to oxa-10.
6SKQ: “Oxa-655_MEM. structural insights into the enhanced carbapenemase efficiency of oxa-655 compared to oxa-10.”. X-ray diffraction, 2 ligands (MER, SO4). MolNFT v1 #164020 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6SKQ
- Type
- protein
- Length
- 980 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A386YIZ1
- Ligands
- MER, SO4
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | — | protein | 245 | — | A0A386YIZ1 |
Ligands and binding sites
- MER · (4R,5S)-3-{[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl}-5-[(2S,3R)-3-hydroxy-1-oxobutan-2-yl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid · ligand · 4 copies · chains A, B, C, D
- SO4 · Sulfate ion · ion · 5 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6SKQ · OXA-655_MEM. Structural insights into the enhanced carbapenemase efficiency of OXA-655… · 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 A0A386YIZ1
- Elsewhere: RCSB PDB 6SKQ · PDBe 6SKQ · UniProt A0A386YIZ1
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