Research workbench

R-hydratase PHAJ1 from pseudomonas aeruginosa in the unliganded form

Analyse R-hydratase PHAJ1 from pseudomonas aeruginosa in the unliganded form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5CPG
Type: protein
Length: 310 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: (R)-specific enoyl-CoA hydratase
EC: 4.2.1.119
UniProt: Q9LBK2
Pockets: 2 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 20% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	(R)-specific enoyl-CoA hydratase (EC 4.2.1.119)	protein	155	20% helix, 36% strand	Q9LBK2

Ligands and binding sites

GOL · Glycerol · additive · 8 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

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	352	0.70	0.82	39	GOL
2	312	0.67	0.81	36	GOL

Interfaces

1 interface between chains.

A–B · 1971 Å² buried · 17 hydrogen bonds · protein-protein

Compared structures

5CPG · R-Hydratase PhaJ1 from Pseudomonas aeruginosa in the unliganded form · 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 Q9LBK2
Elsewhere: RCSB PDB 5CPG · PDBe 5CPG · UniProt Q9LBK2

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