MolNFT v1 · #47900 · protein
Crystal structure of S-adenosylmethionine: 2-dimethylmenaquinone methyltransferase (GK_1813) from geobacillus kaustophilus HTA426
2PCN · S-ADENOSYLMETHIONINE:2-demethylmenaquinone methyltransferase: “Crystal structure of S-adenosylmethionine: 2-dimethylmenaquinone methyltransferase (GK_1813) from geobacillus…”. X-ray diffraction. MolNFT v1 #47900 on GenesisL1: 3D…
- PDB
- 2PCN
- Type
- protein
- Length
- 161 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- S-ADENOSYLMETHIONINE:2-demethylmenaquinone methyltransferase
- EC
- 2.1.1.-
- UniProt
- Q5KYY8
Structure
x-ray diffraction · 1 distinct chain · 20% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | S-ADENOSYLMETHIONINE:2-demethylmenaquinone methyltransferase (EC 2.1.1.-) | protein | 161 | 20% helix, 35% strand | Q5KYY8 |
Ligands and binding sites
- ACT · Acetate ion · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2PCN · Crystal structure of S-adenosylmethionine: 2-dimethylmenaqui methyltransferase (gk_1813)… · 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 Q5KYY8
- Elsewhere: RCSB PDB 2PCN · PDBe 2PCN · UniProt Q5KYY8
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