MolNFT v1 · #85950 · protein

Hafnia alvei phytase in complex with tartrate

4ARU · Histidine acid phosphatase: “Hafnia alvei phytase in complex with tartrate”. X-ray diffraction, 3 ligands (NA, K, CL), 4 pockets (best druggability 0.72). MolNFT v1 #85950 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 4ARU
Type: protein
Length: 405 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Histidine acid phosphatase
EC: 3.1.3.26
UniProt: G9Y2J2
Ligands: NA, K, CL
Pockets: 4 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Histidine acid phosphatase (EC 3.1.3.26)	protein	405	43% helix, 14% strand	G9Y2J2

Ligands and binding sites

NA · Sodium ion · metal · chains A
K · Potassium ion · metal · chains A
CL · Chloride ion · ion · 2 copies · chains A
TLA · L(+)-tartaric acid · additive · 2 copies · chains A

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

Pockets

4 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	673	0.72	0.79	46	TLA, NA
2	57	0.42	0.82	15	empty
3	78	0.42	0.80	16	empty
4	59	0.29	0.75	15	empty

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

4ARU · Hafnia Alvei phytase in complex with tartrate · 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 G9Y2J2
Elsewhere: RCSB PDB 4ARU · PDBe 4ARU · UniProt G9Y2J2

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