MolNFT v1 · #65076 · protein
Crystal structure of protein-disulfide isomerase from novosphingobium aromaticivorans
3GMF: “Crystal structure of protein-disulfide isomerase from novosphingobium aromaticivorans”. X-ray diffraction, 1 ligand (CL), 1 pocket (best druggability 0.27). MolNFT v1 #65076 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 3GMF
- Type
- protein
- Length
- 196 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein-disulfide isomerase
- UniProt
- Q2G9S0
- Ligands
- CL
- Pockets
- 1 · best druggability 0.27
Structure
x-ray diffraction · 1 distinct chain · 58% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein-disulfide isomerase | protein | 196 | 58% helix, 12% strand | Q2G9S0 |
Ligands and binding sites
- CL · Chloride ion · ion · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 50 | 0.27 | 0.74 | 16 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 3GMF · Crystal structure of protein-disulfide isomerase from Novosphingobium aromaticivorans · 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 Q2G9S0
- Elsewhere: RCSB PDB 3GMF · PDBe 3GMF · UniProt Q2G9S0
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