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3U9T

Crystal structure of P. aeruginosa 3-methylcrotonyl-CoA carboxylase (MCC) 750 kD holoenzyme, free enzyme

Functional Information from GO Data
ChainGOidnamespacecontents
A0004485molecular_functionmethylcrotonoyl-CoA carboxylase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0006552biological_processL-leucine catabolic process
A0008300biological_processisoprenoid catabolic process
A0016874molecular_functionligase activity
A0046247biological_processterpene catabolic process
A0046872molecular_functionmetal ion binding
A1905202cellular_componentmethylcrotonoyl-CoA carboxylase complex
B0004485molecular_functionmethylcrotonoyl-CoA carboxylase activity
B0005515molecular_functionprotein binding
B0006552biological_processL-leucine catabolic process
B0008300biological_processisoprenoid catabolic process
B0016874molecular_functionligase activity
B1905202cellular_componentmethylcrotonoyl-CoA carboxylase complex
Functional Information from PROSITE/UniProt
site_idPS00866
Number of Residues15
DetailsCPSASE_1 Carbamoyl-phosphate synthase subdomain signature 1. YPVLLKAAaggGGkG
ChainResidueDetails
ATYR200-GLY214

site_idPS00867
Number of Residues8
DetailsCPSASE_2 Carbamoyl-phosphate synthase subdomain signature 2. FMEMNTRL
ChainResidueDetails
APHE333-LEU340

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PDB entries from 2024-07-24

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