MolNFT v1 · #143025 · protein

Crystal structure of histidinol dehydrogenase from elizabethkingia anophelis

6AN0: “Crystal structure of histidinol dehydrogenase from elizabethkingia anophelis”. X-ray diffraction, 3 ligands (HIS, ZN, IOD), 2 pockets (best druggability 0.71). MolNFT v1 #143025 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 6AN0
Type: protein
Length: 433 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Histidinol dehydrogenase
EC: 1.1.1.23
UniProt: A0A077ECF2
Ligands: HIS, ZN, IOD
Pockets: 2 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Histidinol dehydrogenase (EC 1.1.1.23)	protein	433	47% helix, 17% strand	A0A077ECF2

Ligands and binding sites

HIS · Histidine · ligand · chains A
ZN · Zinc ion · metal · chains A
IOD · Iodide ion · ion · 13 copies · chains A
EDO · 1,2-ethanediol · additive · 5 copies · 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	605	0.71	0.79	65	EDO, IOD
2	76	0.37	0.77	18	IOD, HIS

Compared structures

6AN0 · Crystal Structure of Histidinol Dehydrogenase from Elizabethkingia anophelis · the same entry in another collection · 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 A0A077ECF2
Elsewhere: RCSB PDB 6AN0 · PDBe 6AN0 · UniProt A0A077ECF2

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