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1E3A

A slow processing precursor penicillin acylase from Escherichia coli

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 Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 903
ChainResidue
APRO187
ATHR188
BALA501
BASP531
BHOH2854

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 904
ChainResidue
BSER264
BSER330
BTHR331
BALA332

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 905
ChainResidue
BPHE519
BLEU520
BASN651
BLYS657
BHOH2470
BHOH2856

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 901
ChainResidue
AGLU152
BASP336
BVAL338
BASP339
BPRO468
BASP515

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B 902
ChainResidue
AALA254
AHOH2327
BVAL654
BHOH2464

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile
ChainResidueDetails
BSER264

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING:
ChainResidueDetails
BASP336
BVAL338
BASP339
BPRO468
BASP515

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 841
ChainResidueDetails
BSER264nucleofuge, nucleophile, proton acceptor, proton donor
BALA332electrostatic stabiliser
BASN504electrostatic stabiliser

217705

PDB entries from 2024-03-27

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