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1MBL

A catalytically-impaired class A beta-lactamase: 2 Angstroms crystal structure and kinetics of the Bacillus licheniformis E166A mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0005886cellular_componentplasma membrane
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0030655biological_processbeta-lactam antibiotic catabolic process
A0046677biological_processresponse to antibiotic
B0005886cellular_componentplasma membrane
B0008800molecular_functionbeta-lactamase activity
B0016787molecular_functionhydrolase activity
B0017001biological_processantibiotic catabolic process
B0030655biological_processbeta-lactam antibiotic catabolic process
B0046677biological_processresponse to antibiotic
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 598
ChainResidue
ASER70
ASER130
ALYS234
ATHR235
AGLY236
AALA237
AARG244
AHOH690
AHOH902

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 B 599
ChainResidue
BSER70
BSER130
BTHR216
BTHR235
BGLY236
BALA237
BARG244
BHOH794

site_idCTA
Number of Residues5
Details
ChainResidue
ASER70
ALYS73
ALYS234
ATHR235
ASER130

site_idCTB
Number of Residues5
Details
ChainResidue
BSER130
BSER70
BLYS73
BLYS234
BTHR235

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. FALDTGTNRTVA
ChainResidueDetails
APHE47-ALA59

site_idPS00146
Number of Residues16
DetailsBETA_LACTAMASE_A Beta-lactamase class-A active site. FaFASTiKaltVGVLL
ChainResidueDetails
APHE66-LEU81

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Nucleophile; acyl-ester intermediate","evidences":[{"source":"UniProtKB","id":"P62593","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P62593","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"P62593","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsBinding site: {}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1btl
ChainResidueDetails
AALA166
ALYS73
ASER130
ASER70

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1btl
ChainResidueDetails
BALA166
BLYS73
BSER130
BSER70

249697

PDB entries from 2026-02-25

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