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6WHL

The crystal structure of a beta-lactamase from Legionella pneumophila str. Paris

Functional Information from GO Data
ChainGOidnamespacecontents
A0008658molecular_functionpenicillin binding
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0046677biological_processresponse to antibiotic
B0008658molecular_functionpenicillin binding
B0008800molecular_functionbeta-lactamase activity
B0016787molecular_functionhydrolase activity
B0017001biological_processantibiotic catabolic process
B0046677biological_processresponse to antibiotic
C0008658molecular_functionpenicillin binding
C0008800molecular_functionbeta-lactamase activity
C0016787molecular_functionhydrolase activity
C0017001biological_processantibiotic catabolic process
C0046677biological_processresponse to antibiotic
D0008658molecular_functionpenicillin binding
D0008800molecular_functionbeta-lactamase activity
D0016787molecular_functionhydrolase activity
D0017001biological_processantibiotic catabolic process
D0046677biological_processresponse to antibiotic
E0008658molecular_functionpenicillin binding
E0008800molecular_functionbeta-lactamase activity
E0016787molecular_functionhydrolase activity
E0017001biological_processantibiotic catabolic process
E0046677biological_processresponse to antibiotic
F0008658molecular_functionpenicillin binding
F0008800molecular_functionbeta-lactamase activity
F0016787molecular_functionhydrolase activity
F0017001biological_processantibiotic catabolic process
F0046677biological_processresponse to antibiotic
G0008658molecular_functionpenicillin binding
G0008800molecular_functionbeta-lactamase activity
G0016787molecular_functionhydrolase activity
G0017001biological_processantibiotic catabolic process
G0046677biological_processresponse to antibiotic
H0008658molecular_functionpenicillin binding
H0008800molecular_functionbeta-lactamase activity
H0016787molecular_functionhydrolase activity
H0017001biological_processantibiotic catabolic process
H0046677biological_processresponse to antibiotic
I0008658molecular_functionpenicillin binding
I0008800molecular_functionbeta-lactamase activity
I0016787molecular_functionhydrolase activity
I0017001biological_processantibiotic catabolic process
I0046677biological_processresponse to antibiotic
J0008658molecular_functionpenicillin binding
J0008800molecular_functionbeta-lactamase activity
J0016787molecular_functionhydrolase activity
J0017001biological_processantibiotic catabolic process
J0046677biological_processresponse to antibiotic
K0008658molecular_functionpenicillin binding
K0008800molecular_functionbeta-lactamase activity
K0016787molecular_functionhydrolase activity
K0017001biological_processantibiotic catabolic process
K0046677biological_processresponse to antibiotic
L0008658molecular_functionpenicillin binding
L0008800molecular_functionbeta-lactamase activity
L0016787molecular_functionhydrolase activity
L0017001biological_processantibiotic catabolic process
L0046677biological_processresponse to antibiotic
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue GOL A 301
ChainResidue
ALYS250
AASN251

site_idAC2
Number of Residues3
Detailsbinding site for residue GOL B 301
ChainResidue
BPHE247
BLYS250
BASN251

site_idAC3
Number of Residues2
Detailsbinding site for residue GOL C 301
ChainResidue
CPHE258
DLYS250

site_idAC4
Number of Residues4
Detailsbinding site for residue GOL C 302
ChainResidue
DLEU254
DPHE258
CLYS250
DGLN185

site_idAC5
Number of Residues2
Detailsbinding site for residue GOL E 301
ChainResidue
EPHE247
ELYS250

site_idAC6
Number of Residues4
Detailsbinding site for residue GOL F 301
ChainResidue
ELEU254
FPHE247
FLYS250
FASN251

site_idAC7
Number of Residues3
Detailsbinding site for residue GOL G 301
ChainResidue
GPHE247
GLYS250
GASN251

site_idAC8
Number of Residues3
Detailsbinding site for residue GOL H 301
ChainResidue
HPHE247
HLYS250
HASN251

site_idAC9
Number of Residues4
Detailsbinding site for residue GOL I 301
ChainResidue
IPHE247
ILYS250
IASN251
JLEU254

site_idAD1
Number of Residues3
Detailsbinding site for residue GOL J 301
ChainResidue
JPHE247
JLYS250
JASN251

site_idAD2
Number of Residues3
Detailsbinding site for residue GOL K 301
ChainResidue
KGLN185
LPHE247
LLYS250

site_idAD3
Number of Residues1
Detailsbinding site for residue GOL L 301
ChainResidue
LLEU254

Functional Information from PROSITE/UniProt
site_idPS00337
Number of Residues11
DetailsBETA_LACTAMASE_D Beta-lactamase class-D active site. PaSTFKIAlSL
ChainResidueDetails
APRO47-LEU57

222624

PDB entries from 2024-07-17

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