Research workbench
ATP bound at the active site of a pduo type ATP:CO(I)RRINOID adenosyltransferase from lactobacillus reuteri
Analyse ATP bound at the active site of a pduo type ATP:CO(I)RRINOID… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2NT8
- Type
- protein
- Length
- 181 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cobalamin adenosyltransferase
- EC
- 2.5.1.17
- UniProt
- Q2BVV3
- Ligands
- ATP, MG, SO4
Structure
x-ray diffraction · 1 distinct chain · 60% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cobalamin adenosyltransferase (EC 2.5.1.17) | protein | 181 | 60% helix, 6% strand | Q2BVV3 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · chains A
- MG · Magnesium ion · metal · chains A
- SO4 · Sulfate ion · ion · chains A
- GOL · Glycerol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2NT8 · ATP bound at the active site of a PduO type ATP:co(I)rrinoid adenosyltransferase from… · 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 Q2BVV3
- Elsewhere: RCSB PDB 2NT8 · PDBe 2NT8 · UniProt Q2BVV3
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