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Crystal structure of oxidized hpdi (ABB'XA')

Analyse Crystal structure of oxidized hpdi (ABB'XA') in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4EL1
Type: protein
Length: 904 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein disulfide-isomerase
EC: 5.3.4.1
UniProt: P07237
Pockets: 10 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Protein disulfide-isomerase (EC 5.3.4.1)	protein	452	31% helix, 21% strand	P07237

Pockets

10 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	391	0.59	0.75	46	empty
2	300	0.56	0.77	35	empty
3	247	0.54	0.77	30	empty
4	217	0.49	0.75	31	empty
5	160	0.44	0.74	21	empty

Interfaces

1 interface between chains.

A–B · 958 Å² buried · 17 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

4EL1 · Crystal structure of oxidized hPDI (abb'xa') · the same entry in another collection · chain A against A, TM-score 1.00
P07237 · AlphaFold monomer V2.0 prediction for protein disulfide-isomerase (P07237) · a predicted model of the same protein · chain A against A, TM-score 0.76

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 P07237
Elsewhere: RCSB PDB 4EL1 · PDBe 4EL1 · UniProt P07237

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