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Crystal structure of enoyl-CoA hydratase ECHA1 from mycobacterium marinum

Analyse Crystal structure of enoyl-CoA hydratase ECHA1 from mycobacterium marinum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3QXI
Type: protein
Length: 748 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Enoyl-CoA hydratase ECHA1
EC: 4.2.1.17
UniProt: B2HMZ1
Pockets: 6 · best druggability 0.81

Structure

x-ray diffraction · 2 distinct chains · 45% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Enoyl-CoA hydratase ECHA1 (EC 4.2.1.17)	protein	244	44% helix, 18% strand	B2HMZ1
B, C	Enoyl-CoA hydratase ECHA1 (EC 4.2.1.17)	protein	252	46% helix, 18% strand	B2HMZ1

Pockets

6 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	977	0.81	0.83	92	empty
2	374	0.67	0.80	44	empty
3	324	0.65	0.80	43	empty
4	185	0.59	0.81	27	empty
5	229	0.53	0.76	25	empty

Interfaces

3 interfaces between chains.

B–C · 1573 Å² buried · 11 hydrogen bonds · protein-protein
A–C · 1557 Å² buried · 11 hydrogen bonds · protein-protein
A–B · 1487 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

3QXI · Crystal structure of enoyl-CoA hydratase EchA1 from Mycobacterium marinum · 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 B2HMZ1
Elsewhere: RCSB PDB 3QXI · PDBe 3QXI · UniProt B2HMZ1

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