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Crystal structure of a predicated acyl-CoA synthetase from E.COLI

Analyse Crystal structure of a predicated acyl-CoA synthetase from E.COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3DMY
Type: protein
Length: 893 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein fdra
UniProt: Q47208
Pockets: 10 · best druggability 0.71

Structure

x-ray diffraction · 2 distinct chains · 40% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein fdra	protein	447	41% helix, 21% strand	Q47208
B	Protein fdra	protein	446	40% helix, 21% strand	Q47208

Pockets

10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	522	0.71	0.80	52	empty
2	291	0.64	0.81	46	empty
3	475	0.63	0.77	44	empty
4	218	0.52	0.77	25	empty
5	182	0.50	0.77	23	empty

Interfaces

1 interface between chains.

A–B · 1982 Å² buried · 26 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 20 modified (engineered).

Compared structures

3DMY · Crystal Structure of a predicated acyl-CoA synthetase from E.coli · the same entry in another collection · chain A against A, TM-score 1.00
Q47208 · AlphaFold monomer V2.0 prediction for protein fdra (Q47208) · a predicted model of the same protein · 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 Q47208
Elsewhere: RCSB PDB 3DMY · PDBe 3DMY · UniProt Q47208

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