spacer
spacer

PDBsum entry 8prv

Go to PDB code: 
protein ligands Protein-protein interface(s) links
Cytosolic protein PDB id
8prv

 

 

 

 

Loading ...

 
JSmol PyMol  
Contents
Protein chains
1584 a.a.
163 a.a.
2034 a.a.
Ligands
NAP ×2
A5S
FMN
COA
PDB id:
8prv
Name: Cytosolic protein
Title: Asymmetric unit of the yeast fatty acid synthase in the non-rotated state with acp at the ketosreductase domain (fasamn sample)
Structure: Fatty acid synthase subunit alpha. Chain: a, b. Fatty acid synthase subunit beta. Chain: g. Ec: 2.3.1.86,4.2.1.59,1.3.1.9,2.3.1.38,2.3.1.39,3.1.2.14
Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Organism_taxid: 4932
Authors: K.Singh,G.Bunzel,B.Graf,K.M.Yip,H.Stark,A.Chari
Key ref: K.Singh et al. (2023). Reconstruction of a fatty acid synthesis cycle from a carrier protein and cofactor structural snapshots.. Cell, 186, 5054. PubMed id: 37949058
Date:
12-Jul-23     Release date:   22-Nov-23    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P19097  (FAS2_YEAST) -  Fatty acid synthase subunit alpha from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1887 a.a.
1584 a.a.
Protein chain
Pfam   ArchSchema ?
P19097  (FAS2_YEAST) -  Fatty acid synthase subunit alpha from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1887 a.a.
163 a.a.
Protein chain
Pfam   ArchSchema ?
P07149  (FAS1_YEAST) -  Fatty acid synthase subunit beta from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
2051 a.a.
2034 a.a.*
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class 2: Chains A, B: E.C.1.1.1.100  - 3-oxoacyl-[acyl-carrier-protein] reductase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: a (3R)-hydroxyacyl-[ACP] + NADP+ = a 3-oxoacyl-[ACP] + NADPH + H+
(3R)-hydroxyacyl-[ACP]
+ NADP(+)
= 3-oxoacyl-[ACP]
+ NADPH
+ H(+)
   Enzyme class 3: Chains A, B: E.C.2.3.1.41  - beta-ketoacyl-[acyl-carrier-protein] synthase I.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: a fatty acyl-[ACP] + malonyl-[ACP] + H+ = a 3-oxoacyl-[ACP] + holo- [ACP] + CO2
fatty acyl-[ACP]
+ malonyl-[ACP]
+ H(+)
= 3-oxoacyl-[ACP]
+ holo- [ACP]
+ CO2
   Enzyme class 4: Chains A, B, G: E.C.2.3.1.86  - fatty-acyl-CoA synthase system.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: acetyl-CoA + n malonyl-CoA + 2n NADPH + 4n H+ = a long-chain-acyl-CoA + n CoA + n CO2 + 2n NADP+
acetyl-CoA
+ n malonyl-CoA
+ 2n NADPH
+ 4n H(+)
= long-chain-acyl-CoA
+ n CoA
+ n CO2
+ 2n NADP(+)
   Enzyme class 5: Chain G: E.C.1.3.1.9  - enoyl-[acyl-carrier-protein] reductase (NADH).
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: a 2,3-saturated acyl-[ACP] + NAD+ = a (2E)-enoyl-[ACP] + NADH + H+
2,3-saturated acyl-[ACP]
+ n NAD(+)
= (2E)-enoyl-[ACP]
+ NADH
+ H(+)
   Enzyme class 6: Chain G: E.C.2.3.1.38  - [acyl-carrier-protein] S-acetyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: holo-[ACP] + acetyl-CoA = acetyl-[ACP] + CoA
holo-[ACP]
+ n acetyl-CoA
= acetyl-[ACP]
+ CoA
   Enzyme class 7: Chain G: E.C.2.3.1.39  - [acyl-carrier-protein] S-malonyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: holo-[ACP] + malonyl-CoA = malonyl-[ACP] + CoA
holo-[ACP]
+ n malonyl-CoA
= malonyl-[ACP]
+ CoA
   Enzyme class 8: Chain G: E.C.3.1.2.14  - oleoyl-[acyl-carrier-protein] hydrolase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: (9Z)-octadecenoyl-[ACP] + H2O = (9Z)-octadecenoate + holo-[ACP] + H+
Oleoyl-[acyl-carrier-protein]
+ n H(2)O
= [acyl-carrier-protein]
+ oleate
   Enzyme class 9: Chain G: E.C.4.2.1.59  - 3-hydroxyacyl-[acyl-carrier-protein] dehydratase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O
(3R)-3-hydroxyacyl-[acyl-carrier protein]
= n trans-2-enoyl-[acyl- carrier protein]
+ H(2)O
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 

spacer

spacer