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Structure of POLY(ASPARTIC acid) hydrolase PAHZ2 with GD+3 bound

Analyse Structure of POLY(ASPARTIC acid) hydrolase PAHZ2 with GD+3 bound in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7LJI
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: GD3
Pockets: 4 · best druggability 0.68

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

GD3 · Gadolinium ion · metal · 3 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	495	0.68	0.79	56	empty
2	239	0.48	0.74	34	empty
3	106	0.36	0.74	27	empty
4	85	0.32	0.74	31	empty

Interfaces

1 interface between chains.

A–B · 338 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

7LJI · Structure of poly(aspartic acid) hydrolase PahZ2 with Gd+3 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 7LJI · PDBe 7LJI · UniProt Q769D3

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