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Cryo-EM structure of acp domain from pichia pastoris fatty acid synthase (fas)

Analyse Cryo-EM structure of acp domain from pichia pastoris fatty acid synthase (fas) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7BC5
Type: protein
Length: 161 residues
Chains: 1
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fatty acid synthase subunit alpha
EC: 2.3.1.86, 1.1.1.100, 2.3.1.41
UniProt: C4QY10
Pockets: 1 · best druggability 0.35

Structure

electron microscopy · 1 distinct chain · 42% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fatty acid synthase subunit alpha (EC 2.3.1.86, 1.1.1.100, 2.3.1.41)	protein	161	42% helix, 0% strand	C4QY10

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	86	0.35	0.75	19	empty

Compared structures

7BC5 · Cryo-EM structure of ACP domain from Pichia pastoris fatty acid synthase (FAS) · 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 C4QY10
Elsewhere: RCSB PDB 7BC5 · PDBe 7BC5 · UniProt C4QY10

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