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Crystal structure of a long-chain-fatty-acid-CoA ligase (FADD1) from archaeoglobus fulgidus

Analyse Crystal structure of a long-chain-fatty-acid-CoA ligase (FADD1) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3G7S
Type: protein
Length: 993 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Long-chain-fatty-acid--CoA ligase (fadd-1)
UniProt: O30147
Pockets: 9 · best druggability 0.84

Structure

x-ray diffraction · 2 distinct chains · 32% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Long-chain-fatty-acid--CoA ligase (fadd-1)	protein	497	32% helix, 24% strand	O30147
B	Long-chain-fatty-acid--CoA ligase (fadd-1)	protein	496	32% helix, 24% strand	O30147

Pockets

9 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	213	0.84	0.97	49	empty
2	699	0.72	0.78	72	empty
3	450	0.69	0.80	51	empty
4	662	0.69	0.77	72	empty
5	604	0.68	0.77	56	empty

Interfaces

1 interface between chains.

A–B · 1620 Å² buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 37 modified (engineered).

Compared structures

3G7S · Crystal structure of a long-chain-fatty-acid-CoA ligase (FadD1) from Archaeoglobus… · 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 O30147
Elsewhere: RCSB PDB 3G7S · PDBe 3G7S · UniProt O30147

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