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2FTP

Crystal Structure of hydroxymethylglutaryl-CoA lyase from Pseudomonas aeruginosa

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004419molecular_functionhydroxymethylglutaryl-CoA lyase activity
A0006552biological_processL-leucine catabolic process
A0008300biological_processisoprenoid catabolic process
A0016829molecular_functionlyase activity
A0016833molecular_functionoxo-acid-lyase activity
A0046247biological_processterpene catabolic process
A0046872molecular_functionmetal ion binding
A0046951biological_processketone body biosynthetic process
A0047445molecular_function3-hydroxy-3-isohexenylglutaryl-CoA lyase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 3000
ChainResidue
AASP16
AHIS207
AHIS209
AASN249
AHOH3187

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL A 2000
ChainResidue
AMET59
AALA60
AGLY61
ASER62
AALA63
AASN114
AHOH3167
ASER49
APHE50
AVAL51
APRO53

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 2001
ChainResidue
ALYS54
APHE101
AALA102
AALA103
AASN112
AILE113
ASER143
AHOH3037

Functional Information from PROSITE/UniProt
site_idPS01062
Number of Residues10
DetailsHMG_COA_LYASE Hydroxymethylglutaryl-coenzyme A lyase active site. SVAGLGGCPY
ChainResidueDetails
ASER233-TYR242

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10115
ChainResidueDetails
ACYS240

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AARG15

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305|Ref.4
ChainResidueDetails
AASP16
AHIS207
AHIS209
AASN249

222415

PDB entries from 2024-07-10

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