MolNFT v1 · #38094 · protein
Crystal structure of onconase double mutant with spontaneously- assembled (AMP) 4 stack
2GMK · P-30 protein: “Crystal structure of onconase double mutant with spontaneously- assembled (AMP) 4 stack”. X-ray diffraction, 1 ligand (AMP). MolNFT v1 #38094 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2GMK
- Type
- protein
- Length
- 104 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- P-30 protein
- EC
- 3.1.27.-
- UniProt
- P22069
- Ligands
- AMP
Structure
x-ray diffraction · 1 distinct chain · 19% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | P-30 protein (EC 3.1.27.-) | protein | 104 | 19% helix, 40% strand | P22069 |
Ligands and binding sites
- AMP · Adenosine monophosphate · ligand · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 4 disulfide, 1 modified (disulfide, cyclization).
Compared structures
- 2GMK · Crystal structure of onconase double mutant with spontaneously-assembled (AMP) 4 stack · the same entry in another collection · chain A against A, TM-score 1.00
- P22069 · AlphaFold monomer V2.0 prediction for protein P-30 (P22069) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P22069
- Elsewhere: RCSB PDB 2GMK · PDBe 2GMK · UniProt P22069
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