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1FXH

MUTANT OF PENICILLIN ACYLASE IMPAIRED IN CATALYSIS WITH PHENYLACETIC ACID IN THE ACTIVE SITE

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 Residues6
DetailsBINDING SITE FOR RESIDUE CA B 1002
ChainResidue
AGLU152
BASP73
BVAL75
BASP76
BPRO205
BASP252

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PAC B 1001
ChainResidue
BPHE24
BSER67
BTHR68
BALA69
BHOH1234
AMET142
APHE146
BSER1

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

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING:
ChainResidueDetails
BASP73
BVAL75
BASP76
BPRO205
BASP252

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pnl
ChainResidueDetails
BALA241
BSER1
BALA69

site_idMCSA1
Number of Residues3
DetailsM-CSA 841
ChainResidueDetails
BSER1nucleofuge, nucleophile, proton acceptor, proton donor
BALA69electrostatic stabiliser
BALA241electrostatic stabiliser

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PDB entries from 2024-10-30

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