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5EW0

Crystal structure of the metallo-beta-lactamase Sfh-I in complex with the bisthiazolidine inhibitor L-CS319

Functional Information from GO Data
ChainGOidnamespacecontents
A0008270molecular_functionzinc ion binding
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0042597cellular_componentperiplasmic space
A0046677biological_processresponse to antibiotic
A0046872molecular_functionmetal ion binding
B0008270molecular_functionzinc ion binding
B0008800molecular_functionbeta-lactamase activity
B0016787molecular_functionhydrolase activity
B0017001biological_processantibiotic catabolic process
B0042597cellular_componentperiplasmic space
B0046677biological_processresponse to antibiotic
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue ZN A 301
ChainResidue
AASP111
AARG112
ACYS205
AHIS247
A3C7302

site_idAC2
Number of Residues11
Detailsbinding site for residue 3C7 A 302
ChainResidue
ATHR147
AHIS186
ACYS205
AASN213
APHE216
AHIS247
AZN301
AHIS109
ATHR110
AASP111
APHE146

site_idAC3
Number of Residues5
Detailsbinding site for residue ZN B 301
ChainResidue
BASP111
BCYS205
BHIS247
B3C7302
BHOH406

site_idAC4
Number of Residues14
Detailsbinding site for residue 3C7 B 302
ChainResidue
BTRP80
BHIS109
BTHR110
BASP111
BILE143
BPHE146
BTHR147
BHIS186
BCYS205
BASN213
BPHE216
BHIS247
BZN301
BHOH406

Functional Information from PROSITE/UniProt
site_idPS00743
Number of Residues20
DetailsBETA_LACTAMASE_B_1 Beta-lactamases class B signature 1. InTNyHTDraGGnaywktl.G
ChainResidueDetails
AILE104-GLY123

site_idPS00744
Number of Residues13
DetailsBETA_LACTAMASE_B_2 Beta-lactamases class B signature 2. PaerVLyGnCILK
ChainResidueDetails
APRO196-LYS208

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PDB entries from 2024-06-12

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