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2AE4

Glutaryl 7-Aminocephalosporanic Acid Acylase: mutational study of activation mechanism

Functional Information from GO Data
ChainGOidnamespacecontents
A0016787molecular_functionhydrolase activity
A0016811molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
A0017000biological_processantibiotic biosynthetic process
B0016787molecular_functionhydrolase activity
B0017000biological_processantibiotic biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 B 529
ChainResidue
ATYR149
BSER1
BTYR33
BGLN50
BARG57
BPHE58
BASN68
BVAL70
BPHE177

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 401
ChainResidue
ALEU148
ASER152
APRO162
AHOH475
AHOH478
BTYR30
BPHE31

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile
ChainResidueDetails
BSER1

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000255
ChainResidueDetails
BHIS23
BGLU455

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 3s8r
ChainResidueDetails
BSER1
BASN244
BVAL70

site_idMCSA1
Number of Residues5
DetailsM-CSA 288
ChainResidueDetails
BSER1activator, covalently attached, hydrogen bond acceptor, hydrogen bond donor, increase electrophilicity, nucleofuge, nucleophile, polar interaction, proton acceptor, proton donor
BHIS23activator, electrostatic stabiliser, increase acidity, steric role
BVAL70electrostatic stabiliser
BASN244electrostatic stabiliser
BGLU455activator, electrostatic stabiliser, increase acidity, steric role

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PDB entries from 2024-09-04

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