MolNFT v1 · #6707 · protein

Murine adenosine deaminase (D296A)

1FKX: “Murine adenosine deaminase (D296A)”. X-ray diffraction, 2 ligands (PRH, ZN), 2 pockets (best druggability 0.66). MolNFT v1 #6707 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1FKX
Type: protein
Length: 349 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Adenosine deaminase
EC: 3.5.4.4
UniProt: P03958
Ligands: PRH, ZN
Pockets: 2 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 52% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Adenosine deaminase (EC 3.5.4.4)	protein	349	52% helix, 15% strand	P03958

Ligands and binding sites

PRH · 6-hydroxy-1,6-dihydro purine nucleoside · ligand · chains A
ZN · Zinc ion · metal · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	192	0.66	0.85	30	PRH
2	101	0.40	0.77	17	empty

Compared structures

1FKX · Murine adenosine deaminase (D296A) · the same entry in another collection · chain A against A, TM-score 1.00
P03958 · AlphaFold monomer V2.0 prediction for adenosine deaminase (P03958) · a predicted model of the same protein · 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 P03958
Elsewhere: RCSB PDB 1FKX · PDBe 1FKX · UniProt P03958

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