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1H2G

Altered substrate specificity mutant of penicillin acylase

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 1558
ChainResidue
AGLU152
BASP73
BVAL75
BASP76
BPRO205
BASP252

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 1208
ChainResidue
BSER508
BPHE510
BASP518
AGLN37
AASP38
AHOH2172

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 1559
ChainResidue
BASN241
BLEU257
BASN388
BLYS394
BHOH2193
BHOH2289

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 1560
ChainResidue
BASP327
BILE329
BHOH2422
BHOH2423

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 1561
ChainResidue
AMET142
BSER1
BTHR68
BALA69
BHOH2424

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
BPRO205
BASP252
BASP73
BVAL75
BASP76

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 841
ChainResidueDetails
BALA69electrostatic stabiliser
BASN241electrostatic stabiliser
BSER1nucleofuge, nucleophile, proton acceptor, proton donor

221051

PDB entries from 2024-06-12

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