MolNFT v1 · #115524 · protein
Gta mutant with mercury - E303A
5CMF · Histo-blood group abo system transferase: “Gta mutant with mercury - E303A”. X-ray diffraction, 1 ligand (HG), 1 pocket (best druggability 0.58). MolNFT v1 #115524 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5CMF
- Type
- protein
- Length
- 263 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histo-blood group abo system transferase
- EC
- 2.4.1.40, 2.4.1.37
- UniProt
- P16442
- Ligands
- HG
- Pockets
- 1 · best druggability 0.58
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X | Histo-blood group abo system transferase (EC 2.4.1.40, 2.4.1.37) | protein | 263 | 31% helix, 23% strand | P16442 |
Ligands and binding sites
- HG · Mercury (II) ion · metal · 4 copies · chains X
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 351 | 0.58 | 0.76 | 39 | HG |
Compared structures
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 P16442
- Elsewhere: RCSB PDB 5CMF · PDBe 5CMF · UniProt P16442
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