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Structure of the class C acid phosphatase from pasteurella multocida

Analyse Structure of the class C acid phosphatase from pasteurella multocida in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3PCT
Type: protein
Length: 754 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Class C acid phosphatase
EC: 3.1.3.2
UniProt: B9VWB2
Pockets: 9 · best druggability 0.74

Structure

x-ray diffraction · 3 distinct chains · 51% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Class C acid phosphatase (EC 3.1.3.2)	protein	246	51% helix, 14% strand	B9VWB2
B	Class C acid phosphatase (EC 3.1.3.2)	protein	253	50% helix, 14% strand	B9VWB2
C	Class C acid phosphatase (EC 3.1.3.2)	protein	255	51% helix, 14% strand	B9VWB2

Pockets

9 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	0.74	0.82	56	empty
2	500	0.71	0.80	51	empty
3	155	0.69	0.89	33	empty
4	188	0.64	0.85	28	empty
5	114	0.40	0.75	18	empty

Interfaces

2 interfaces between chains.

A–B · 3037 Å² buried · 42 hydrogen bonds · protein-protein
A–C · 476 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

3PCT · Structure of the class C acid phosphatase from Pasteurella multocida · 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 B9VWB2
Elsewhere: RCSB PDB 3PCT · PDBe 3PCT · UniProt B9VWB2

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