MolNFT v1 · #40027 · protein
P. aeruginosa azurin N42C/M64E double mutant, bmme-linked dimer
2IDF: “P. aeruginosa azurin N42C/M64E double mutant, bmme-linked dimer”. X-ray diffraction, 3 ligands (OPP, CU, NI). MolNFT v1 #40027 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2IDF
- Type
- protein
- Length
- 256 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Azurin
- UniProt
- P00282
- Ligands
- OPP, CU, NI
Structure
x-ray diffraction · 1 distinct chain · 19% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Azurin | protein | 128 | 19% helix, 34% strand | P00282 |
Ligands and binding sites
- OPP · 1-[pyrrol-1-yl-2,5-dione-methoxymethyl]-pyrrole-2,5-dione · ligand · chains A, B
- CU · Copper (II) ion · metal · 2 copies · chains A, B
- NI · Nickel (II) ion · metal · 2 copies · chains A, B
- 144 · Tris-hydroxymethyl-methyl-ammonium · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 463 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent, 2 disulfide (covalent ligand, disulfide).
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 P00282
- Elsewhere: RCSB PDB 2IDF · PDBe 2IDF · UniProt P00282
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