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Crystal structure of a putative enoyl-CoA HYDRATASE/ISOMERASE from acinetobacter baumannii

Analyse Crystal structure of a putative enoyl-CoA HYDRATASE/ISOMERASE from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3FDU
Type: protein
Length: 1,381 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative enoyl-CoA HYDRATASE/ISOMERASE
UniProt: A3M7S1
Ligands: SO4
Pockets: 15 · best druggability 0.84

Structure

x-ray diffraction · 6 distinct chains · 51% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative enoyl-CoA HYDRATASE/ISOMERASE	protein	248	52% helix, 16% strand	A3M7S1
B	Putative enoyl-CoA HYDRATASE/ISOMERASE	protein	232	52% helix, 17% strand	A3M7S1
C	Putative enoyl-CoA HYDRATASE/ISOMERASE	protein	227	49% helix, 18% strand	A3M7S1
D	Putative enoyl-CoA HYDRATASE/ISOMERASE	protein	225	50% helix, 18% strand	A3M7S1
E	Putative enoyl-CoA HYDRATASE/ISOMERASE	protein	234	53% helix, 17% strand	A3M7S1
F	Putative enoyl-CoA HYDRATASE/ISOMERASE	protein	215	50% helix, 19% strand	A3M7S1

Ligands and binding sites

SO4 · Sulfate ion · ion · 4 copies · chains A, C, E
GOL · Glycerol · additive · chains A

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

Pockets

15 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1072	0.84	0.85	127	SO4
2	586	0.80	0.85	70	empty
3	541	0.70	0.80	57	empty
4	548	0.70	0.80	57	empty
5	113	0.64	0.87	27	GOL

Interfaces

8 interfaces between chains.

E–F · 1094 Å² buried · 15 hydrogen bonds · protein-protein
B–C · 1089 Å² buried · 15 hydrogen bonds · protein-protein
A–B · 1085 Å² buried · 14 hydrogen bonds · protein-protein
A–C · 1080 Å² buried · 14 hydrogen bonds · protein-protein
D–E · 1067 Å² buried · 16 hydrogen bonds · protein-protein

Compared structures

3FDU · Crystal structure of a putative enoyl-CoA hydratase/isomerase from Acinetobacter baumannii · 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 A3M7S1
Elsewhere: RCSB PDB 3FDU · PDBe 3FDU · UniProt A3M7S1

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