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6NHU

Crystal Structure of the Beta Lactamase Class D YbxI from Agrobacterium fabrum

Functional Information from GO Data
ChainGOidnamespacecontents
A0008658molecular_functionpenicillin binding
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0046677biological_processresponse to antibiotic
A0071555biological_processcell wall organization
B0008658molecular_functionpenicillin binding
B0008800molecular_functionbeta-lactamase activity
B0016787molecular_functionhydrolase activity
B0017001biological_processantibiotic catabolic process
B0046677biological_processresponse to antibiotic
B0071555biological_processcell wall organization
C0008658molecular_functionpenicillin binding
C0008800molecular_functionbeta-lactamase activity
C0016787molecular_functionhydrolase activity
C0017001biological_processantibiotic catabolic process
C0046677biological_processresponse to antibiotic
C0071555biological_processcell wall organization
D0008658molecular_functionpenicillin binding
D0008800molecular_functionbeta-lactamase activity
D0016787molecular_functionhydrolase activity
D0017001biological_processantibiotic catabolic process
D0046677biological_processresponse to antibiotic
D0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue GOL A 301
ChainResidue
ASER60
ALYS63
AASP108
ALYS206
AGLY208
ATHR209

site_idAC2
Number of Residues8
Detailsbinding site for residue PO4 B 300
ChainResidue
DASP196
DALA197
DPRO198
DGLU199
DSER200
BARG93
BTYR211
BEDO302

site_idAC3
Number of Residues6
Detailsbinding site for residue EDO B 301
ChainResidue
BLYS80
BTHR81
BPRO82
BALA83
BHOH407
CARG97

site_idAC4
Number of Residues5
Detailsbinding site for residue EDO B 302
ChainResidue
BTYR211
BARG213
BPRO219
BPO4300
DGLU199

site_idAC5
Number of Residues8
Detailsbinding site for residue PO4 C 300
ChainResidue
AARG93
ATHR209
ATYR211
CALA197
CPRO198
CGLU199
CSER200
CHOH409

site_idAC6
Number of Residues4
Detailsbinding site for residue EDO C 301
ChainResidue
CASP85
CLYS87
CTHR90
CTRP112

site_idAC7
Number of Residues5
Detailsbinding site for residue EDO D 301
ChainResidue
DASP85
DLYS87
DTHR90
DTRP112
DGLU116

Functional Information from PROSITE/UniProt
site_idPS00337
Number of Residues11
DetailsBETA_LACTAMASE_D Beta-lactamase class-D active site. PaSTFKVPlAL
ChainResidueDetails
APRO58-LEU68

225946

PDB entries from 2024-10-09

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