Research workbench
B. pseudomallei katg crystalized in the presence of abts
Analyse B. pseudomallei katg crystalized in the presence of abts in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6MQ1
- Type
- protein
- Length
- 1,424 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A095KYK6
- Ligands
- HEM, NA, CL, PO4, OXY
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 712 | — | A0A095KYK6 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
- NA · Sodium ion · metal · 2 copies · chains A, B
- CL · Chloride ion · ion · chains A, B
- PO4 · Phosphate ion · ion · chains A
- OXY · Oxygen molecule · ion · chains B
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6MQ1 · B. pseudomallei KatG crystalized in the presence of ABTS · 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 A0A095KYK6
- Elsewhere: RCSB PDB 6MQ1 · PDBe 6MQ1 · UniProt A0A095KYK6
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