MolNFT v1 · #16364 · protein

Crystallographic study of azurin from pseudomonas putida

1NWP: “Crystallographic study of azurin from pseudomonas putida”. X-ray diffraction, 2 ligands (ZN, CU), 2 pockets (best druggability 0.41). MolNFT v1 #16364 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1NWP
Type: protein
Length: 256 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Azurin
UniProt: P34097
Ligands: ZN, CU
Pockets: 2 · best druggability 0.41

Structure

x-ray diffraction · 1 distinct chain · 19% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Azurin	protein	128	19% helix, 36% strand	P34097

Ligands and binding sites

ZN · Zinc ion · metal · 4 copies · chains A, B
CU · Copper (II) ion · metal · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	65	0.41	0.80	17	empty
2	90	0.39	0.77	23	empty

Interfaces

1 interface between chains.

A–B · 478 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

1NWP · Crystallographic study of azurin from pseudomonas putida · the same entry in another collection · chain A against A, TM-score 1.00
P34097 · AlphaFold monomer V2.0 prediction for azurin (P34097) · a predicted model of the same protein · chain B against A, TM-score 0.99

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 P34097
Elsewhere: RCSB PDB 1NWP · PDBe 1NWP · UniProt P34097

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