Research workbench
Acinetobacter baumannii undecaprenyl pyrophosphate synthase (ab-upps) in complex with GR839 and GSK513
Analyse Acinetobacter baumannii undecaprenyl pyrophosphate synthase (ab-upps) in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6SZG
- Type
- protein
- Length
- 435 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- V5VCK8
- Ligands
- M2K, M2E, CA
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 222 | — | V5VCK8 |
| B | — | protein | 213 | — | V5VCK8 |
Ligands and binding sites
- M2K · 4,5,6,7-tetrahydro-2~{H}-indazole-3-carboxylic acid · ligand · chains A
- M2E · (4-chlorophenyl)-[(3~{S})-3-oxidanylpiperidin-1-yl]methanone · ligand · chains A
- CA · Calcium ion · metal · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6SZG · Acinetobacter baumannii undecaprenyl pyrophosphate synthase (AB-UppS) in complex with… · 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 V5VCK8
- Elsewhere: RCSB PDB 6SZG · PDBe 6SZG · UniProt V5VCK8
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