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Human ACYLPHOSPHATASE(ACPH) surface charge-optimized

Analyse Human ACYLPHOSPHATASE(ACPH) surface charge-optimized in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2K7J
Type: protein
Length: 99 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Acylphosphatase-1
EC: 3.6.1.7
UniProt: P07311
Pockets: 1 · best druggability 0.45

Structure

solution nmr · 1 distinct chain · 23% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Acylphosphatase-1 (EC 3.6.1.7)	protein	99	23% helix, 25% strand	P07311

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	64	0.45	0.82	14	empty

Compared structures

2K7J · Human Acylphosphatase(AcPh) surface charge-optimized · the same entry in another collection · chain A against A, TM-score 1.00
P07311 · AlphaFold monomer V2.0 prediction for acylphosphatase-1 (P07311) · a predicted model of the same protein · chain A against A, TM-score 0.89

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 P07311
Elsewhere: RCSB PDB 2K7J · PDBe 2K7J · UniProt P07311

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