MolNFT v1 · #32774 · protein

Structure of pdi-related chaperone, wind with his-tag on C-terminus.

2C0E · Windbeutel protein: “Structure of pdi-related chaperone, wind with his-tag on C-terminus.”. X-ray diffraction, 4 pockets (best druggability 0.51). MolNFT v1 #32774 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2C0E
Type: protein
Length: 452 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Windbeutel protein
UniProt: O44342
Pockets: 4 · best druggability 0.51

Structure

x-ray diffraction · 2 distinct chains · 50% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Windbeutel protein	protein	228	50% helix, 11% strand	O44342
B	Windbeutel protein	protein	224	50% helix, 12% strand	O44342

Pockets

4 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	267	0.51	0.75	41	empty
2	147	0.46	0.77	27	empty
3	61	0.35	0.78	18	empty
4	79	0.34	0.75	19	empty

Interfaces

1 interface between chains.

A–B · 778 Å² buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

2C0E · Structure of PDI-related Chaperone, Wind with his-tag on C-terminus. · 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 0.94

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 2C0E · PDBe 2C0E · UniProt O44342

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