MolNFT v1 · #7898 · protein

Histidine ammonia-lyase (hal) mutant Y280F from pseudomonas putida

1GKJ: “Histidine ammonia-lyase (hal) mutant Y280F from pseudomonas putida”. X-ray diffraction, 1 ligand (SO4), 2 pockets (best druggability 0.31). MolNFT v1 #7898 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1GKJ
Type: protein
Length: 507 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Histidine ammonia-lyase
EC: 4.3.1.3
UniProt: P21310
Ligands: SO4
Pockets: 2 · best druggability 0.31

Structure

x-ray diffraction · 1 distinct chain · 58% helix, 7% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Histidine ammonia-lyase (EC 4.3.1.3)	protein	507	58% helix, 7% strand	P21310

Ligands and binding sites

SO4 · Sulfate ion · ion · chains A
GOL · Glycerol · additive · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	60	0.31	0.75	15	SO4
2	59	0.28	0.74	15	empty

Modifications

Observed in the structure: 1 modified (nonstandard).

Compared structures

1GKJ · Histidine Ammonia-Lyase (HAL) Mutant Y280F from Pseudomonas putida · the same entry in another collection · chain A against A, TM-score 1.00
P21310 · AlphaFold monomer V2.0 prediction for histidine ammonia-lyase (P21310) · a predicted model of the same protein · chain A 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 P21310
Elsewhere: RCSB PDB 1GKJ · PDBe 1GKJ · UniProt P21310

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.