MolNFT v1 · #181070 · protein

Structure of POLY(ASPARTIC acid) hydrolase PAHZ2 with ZN+2 bound

7LJH: “Structure of POLY(ASPARTIC acid) hydrolase PAHZ2 with ZN+2 bound”. X-ray diffraction, 1 ligand (ZN), 4 pockets (best druggability 0.67). MolNFT v1 #181070 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7LJH
Type: protein
Length: 800 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: POLY(ASPARTIC acid) hydrolase
UniProt: Q769D3
Ligands: ZN
Pockets: 4 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	POLY(ASPARTIC acid) hydrolase	protein	400	37% helix, 27% strand	Q769D3

Ligands and binding sites

ZN · Zinc ion · metal · 28 copies · chains A, B

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	500	0.67	0.78	60	empty
2	182	0.44	0.74	27	empty
3	141	0.40	0.75	31	ZN
4	134	0.38	0.74	31	ZN

Interfaces

1 interface between chains.

A–B · 330 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

7LJH · Structure of poly(aspartic acid) hydrolase PahZ2 with Zn+2 bound · 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 Q769D3
Elsewhere: RCSB PDB 7LJH · PDBe 7LJH · UniProt Q769D3

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