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Crystal structure of acid phosphatase

Analyse Crystal structure of acid phosphatase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7F17
Type: protein
Length: 636 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Acid phosphatase
EC: 3.1.3.2
UniProt: A0A0D6FFE3
Pockets: 12 · best druggability 0.64

Structure

x-ray diffraction · 3 distinct chains · 65% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Acid phosphatase (EC 3.1.3.2)	protein	212	64% helix, 0% strand	A0A0D6FFE3
B	Acid phosphatase (EC 3.1.3.2)	protein	213	66% helix, 0% strand	A0A0D6FFE3
C	Acid phosphatase (EC 3.1.3.2)	protein	211	65% helix, 0% strand	A0A0D6FFE3

Pockets

12 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	499	0.64	0.77	55	empty
2	324	0.57	0.76	29	empty
3	333	0.56	0.75	39	empty
4	166	0.50	0.78	22	empty
5	178	0.47	0.75	22	empty

Interfaces

2 interfaces between chains.

B–C · 1004 Å² buried · 8 hydrogen bonds · protein-protein
A–B · 466 Å² buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 9 modified (engineered).

Compared structures

7F17 · Crystal Structure of acid phosphatase · 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 A0A0D6FFE3
Elsewhere: RCSB PDB 7F17 · PDBe 7F17 · UniProt A0A0D6FFE3

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