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1FXV

PENICILLIN ACYLASE MUTANT IMPAIRED IN CATALYSIS WITH PENICILLIN G 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 Residues11
DetailsBINDING SITE FOR RESIDUE PNN B 1001
ChainResidue
AMET142
BHOH2215
BHOH2216
APHE146
ASER149
BSER1
BGLN23
BPHE24
BTHR68
BALA69
BPHE71

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 2001
ChainResidue
AGLU152
BASP73
BVAL75
BASP76
BPRO205
BASP252

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 2024-05-01

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