Research workbench
Mycobacterium tuberculosis pduo-type ATP:COBALAMIN adenosyltransferase bound to adenosylcobalamin
Analyse Mycobacterium tuberculosis pduo-type ATP:COBALAMIN adenosyltransferase bound to… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6WGS
- Type
- protein
- Length
- 177 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Corrinoid adenosyltransferase
- EC
- 2.5.1.17
- UniProt
- A0A045JVI3
- Ligands
- B12, 5AD
Structure
x-ray diffraction · 1 distinct chain · 59% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Corrinoid adenosyltransferase (EC 2.5.1.17) | protein | 177 | 59% helix, 5% strand | A0A045JVI3 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6WGS · Mycobacterium tuberculosis pduO-type ATP:cobalamin adenosyltransferase bound to… · 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 A0A045JVI3
- Elsewhere: RCSB PDB 6WGS · PDBe 6WGS · UniProt A0A045JVI3
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