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Structure of the fungal type I fas ppt domain

Analyse Structure of the fungal type I fas ppt domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2WAS
Type: protein
Length: 661 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 3-oxoacyl-[acyl-carrier-protein] synthase
EC: 2.7.8.7, 2.3.1.41
UniProt: P19097
Pockets: 12 · best druggability 0.60

Structure

x-ray diffraction · 6 distinct chains · 40% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	3-oxoacyl-[acyl-carrier-protein] synthase (EC 2.7.8.7, 2.3.1.41)	protein	113	40% helix, 33% strand	P19097
B	3-oxoacyl-[acyl-carrier-protein] synthase (EC 2.7.8.7, 2.3.1.41)	protein	118	38% helix, 27% strand	P19097
C	3-oxoacyl-[acyl-carrier-protein] synthase (EC 2.7.8.7, 2.3.1.41)	protein	111	41% helix, 29% strand	P19097
D	3-oxoacyl-[acyl-carrier-protein] synthase (EC 2.7.8.7, 2.3.1.41)	protein	107	41% helix, 28% strand	P19097
E	3-oxoacyl-[acyl-carrier-protein] synthase (EC 2.7.8.7, 2.3.1.41)	protein	106	42% helix, 30% strand	P19097
F	3-oxoacyl-[acyl-carrier-protein] synthase (EC 2.7.8.7, 2.3.1.41)	protein	106	42% helix, 32% strand	P19097

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	368	0.60	0.77	45	empty
2	205	0.49	0.76	27	empty
3	179	0.48	0.76	23	empty
4	175	0.45	0.75	32	empty
5	158	0.45	0.76	23	empty

Interfaces

13 interfaces between chains.

B–C · 623 Å² buried · 6 hydrogen bonds · protein-protein
A–B · 565 Å² buried · 6 hydrogen bonds · protein-protein
A–C · 554 Å² buried · 7 hydrogen bonds · protein-protein
D–E · 535 Å² buried · 6 hydrogen bonds · protein-protein
E–F · 533 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

2WAS · Structure of the fungal type I FAS PPT domain · the same entry in another collection · chain F against F, TM-score 1.00
P19097 · AlphaFold monomer V2.0 prediction for fatty acid synthase subunit alpha (P19097) · a predicted model of the same protein · chain E against A, TM-score 0.98

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 P19097
Elsewhere: RCSB PDB 2WAS · PDBe 2WAS · UniProt P19097

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