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Apo-form piga

Analyse Apo-form piga in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5ZW0
Type: protein
Length: 757 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: L-prolyl-[peptidyl-carrier protein] dehydrogenase
EC: 1.3.8.14
UniProt: Q5W271
Pockets: 10 · best druggability 0.65

Structure

x-ray diffraction · 2 distinct chains · 57% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	L-prolyl-[peptidyl-carrier protein] dehydrogenase (EC 1.3.8.14)	protein	382	56% helix, 15% strand	Q5W271
B	L-prolyl-[peptidyl-carrier protein] dehydrogenase (EC 1.3.8.14)	protein	375	57% helix, 16% strand	Q5W271

Pockets

10 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	354	0.65	0.79	43	empty
2	339	0.64	0.79	43	empty
3	92	0.62	0.89	19	empty
4	80	0.61	0.89	18	empty
5	242	0.54	0.76	30	empty

Interfaces

1 interface between chains.

A–B · 2160 Å² buried · 18 hydrogen bonds · protein-protein

Compared structures

5ZW0 · Apo-form PigA · the same entry in another collection · chain A against A, TM-score 1.00
Q5W271 · AlphaFold monomer V2.0 prediction for L-prolyl-[peptidyl-carrier protein] dehydrogenase… · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q5W271
Elsewhere: RCSB PDB 5ZW0 · PDBe 5ZW0 · UniProt Q5W271

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