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Structure of prgx Y153C mutant

Analyse Structure of prgx Y153C mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2AXV
Type: protein
Length: 1,209 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Prgx
UniProt: Q04114
Pockets: 14 · best druggability 0.83

Structure

x-ray diffraction · 2 distinct chains · 74% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C, D	Prgx	protein	302	74% helix, 1% strand	Q04114
B	Prgx	protein	303	74% helix, 1% strand	Q04114

Pockets

14 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	1142	0.83	0.84	116	empty
2	1025	0.83	0.84	110	empty
3	824	0.67	0.74	58	empty
4	182	0.54	0.79	28	empty
5	92	0.50	0.82	22	empty

Interfaces

4 interfaces between chains.

C–D · 3018 Å² buried · 39 hydrogen bonds · protein-protein
A–B · 2974 Å² buried · 46 hydrogen bonds · protein-protein
A–C · 521 Å² buried · 13 hydrogen bonds · protein-protein
B–D · 511 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

2AXV · Structure of PrgX Y153C mutant · 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 Q04114
Elsewhere: RCSB PDB 2AXV · PDBe 2AXV · UniProt Q04114

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