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Structure of pdi-related chaperone, wind mutant-Y55K

Analyse Structure of pdi-related chaperone, wind mutant-Y55K in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2C1Y
Type: protein
Length: 359 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Windbeutel protein
UniProt: O44342
Pockets: 2 · best druggability 0.55

Structure

x-ray diffraction · 2 distinct chains · 43% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Windbeutel protein	protein	231	51% helix, 11% strand	O44342
B	Windbeutel protein	protein	128	29% helix, 19% strand	O44342

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	299	0.55	0.76	44	empty
2	129	0.38	0.74	24	empty

Interfaces

1 interface between chains.

A–B · 830 Å² buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

2C1Y · Structure of PDI-related Chaperone, Wind mutant-Y55K · the same entry in another collection · chain A against A, TM-score 1.00
O44342 · AlphaFold monomer V2.0 prediction for protein windbeutel (O44342) · a predicted model of the same protein · chain B 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 O44342
Elsewhere: RCSB PDB 2C1Y · PDBe 2C1Y · UniProt O44342

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