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Crystal strcuture of feruloyl-CoA hydratase LYASE(FCHL) from pseudomonas putida KT2440

Analyse Crystal strcuture of feruloyl-CoA hydratase LYASE(FCHL) from pseudomonas putida… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6L3O
Type: protein
Length: 497 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hydroxycinnamoyl-CoA hydratase-lyase
EC: 4.1.2.41, 4.2.1.101
UniProt: Q88HJ8
Pockets: 8 · best druggability 0.73

Structure

x-ray diffraction · 2 distinct chains · 53% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hydroxycinnamoyl-CoA hydratase-lyase (EC 4.1.2.41, 4.2.1.101)	protein	248	54% helix, 18% strand	Q88HJ8
B	Hydroxycinnamoyl-CoA hydratase-lyase (EC 4.1.2.41, 4.2.1.101)	protein	249	53% helix, 18% strand	Q88HJ8

Pockets

8 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	685	0.73	0.79	56	empty
2	272	0.65	0.82	32	empty
3	288	0.63	0.80	33	empty
4	207	0.56	0.79	30	empty
5	192	0.54	0.79	25	empty

Interfaces

1 interface between chains.

A–B · 850 Å² buried · 15 hydrogen bonds · protein-protein

Compared structures

6L3O · Crystal strcuture of Feruloyl-CoA hydratase lyase(FCHL) from Pseudomonas putida KT2440 · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q88HJ8
Elsewhere: RCSB PDB 6L3O · PDBe 6L3O · UniProt Q88HJ8

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