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3Q6V

Crystal Structure of Serratia fonticola Sfh-I: glycerol complex

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 Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 1
ChainResidue
AHIS118
AASP120
AHIS196
ACYS221
AASN233
AHIS263
AHOH281
AHOH283
AZN2

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 2
ChainResidue
AGOL1
AASP120
ACYS221
AHIS263

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL B 1
ChainResidue
BZN2
BHIS118
BASP120
BHIS196
BCYS221
BASN233
BHIS263
BHOH353
BHOH504

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 2
ChainResidue
BGOL1
BASP120
BCYS221
BHIS263

Functional Information from PROSITE/UniProt
site_idPS00743
Number of Residues20
DetailsBETA_LACTAMASE_B_1 Beta-lactamases class B signature 1. InTNyHTDraGGnaywktl.G
ChainResidueDetails
AILE113-GLY133

site_idPS00744
Number of Residues13
DetailsBETA_LACTAMASE_B_2 Beta-lactamases class B signature 2. PaerVLyGnCILK
ChainResidueDetails
APRO209-LYS224

224572

PDB entries from 2024-09-04

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