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Three-dimensional structure of the C65A-K59A double mutant of human lipocalin-type prostaglandin D synthase apo-form

Analyse Three-dimensional structure of the C65A-K59A double mutant of human… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4ORW
Type: protein
Length: 318 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Prostaglandin-H2 D-isomerase
EC: 5.3.99.2
UniProt: P41222
Pockets: 2 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 19% helix, 48% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Prostaglandin-H2 D-isomerase (EC 5.3.99.2)	protein	159	19% helix, 48% strand	P41222

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	595	0.78	0.83	44	empty
2	555	0.75	0.82	44	empty

Interfaces

1 interface between chains.

A–B · 457 Å² buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

4ORW · Three-dimensional structure of the C65A-K59A double mutant of Human lipocalin-type… · the same entry in another collection · chain A against A, TM-score 1.00
P41222 · AlphaFold monomer V2.0 prediction for prostaglandin-H2 D-isomerase (P41222) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P41222
Elsewhere: RCSB PDB 4ORW · PDBe 4ORW · UniProt P41222

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