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7ZZ3

Cryo-EM structure of "BC react" conformation of Lactococcus lactis pyruvate carboxylase with acetyl-CoA

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004736molecular_functionpyruvate carboxylase activity
A0005524molecular_functionATP binding
A0006090biological_processpyruvate metabolic process
A0006094biological_processgluconeogenesis
A0046872molecular_functionmetal ion binding
B0003824molecular_functioncatalytic activity
B0004736molecular_functionpyruvate carboxylase activity
B0005524molecular_functionATP binding
B0006090biological_processpyruvate metabolic process
B0006094biological_processgluconeogenesis
B0046872molecular_functionmetal ion binding
C0003824molecular_functioncatalytic activity
C0004736molecular_functionpyruvate carboxylase activity
C0005524molecular_functionATP binding
C0006090biological_processpyruvate metabolic process
C0006094biological_processgluconeogenesis
C0046872molecular_functionmetal ion binding
D0003824molecular_functioncatalytic activity
D0004736molecular_functionpyruvate carboxylase activity
D0005524molecular_functionATP binding
D0006090biological_processpyruvate metabolic process
D0006094biological_processgluconeogenesis
D0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00866
Number of Residues15
DetailsCPSASE_1 Carbamoyl-phosphate synthase subdomain signature 1. YPVMIKAAlggGGrG
ChainResidueDetails
ATYR152-GLY166

site_idPS00867
Number of Residues8
DetailsCPSASE_2 Carbamoyl-phosphate synthase subdomain signature 2. FIEVNPRV
ChainResidueDetails
APHE284-VAL291

226707

PDB entries from 2024-10-30

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