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6XFR

Metallo-beta-lactamase from Pontibacter korlensis

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 Residues7
Detailsbinding site for residue EPE A 301
ChainResidue
ATHR124
AGLU133
ATYR149
AARG191
ATYR192
APRO193
ALYS194

site_idAC2
Number of Residues7
Detailsbinding site for residue EPE A 302
ChainResidue
AGLY171
AASN172
AHIS202
AZN307
AHOH413
ATYR26
ATRP51

site_idAC3
Number of Residues10
Detailsbinding site for residue EPE A 303
ChainResidue
ALYS41
AGLU42
AGLY43
AGLN69
APRO70
BGLU54
BGLU57
BGLU58
BLEU60
BTHR61

site_idAC4
Number of Residues5
Detailsbinding site for residue ZN A 304
ChainResidue
AASP82
ACYS160
AHIS202
AZN305
AHOH409

site_idAC5
Number of Residues5
Detailsbinding site for residue ZN A 305
ChainResidue
AHIS78
AHIS80
AHIS141
AZN304
AHOH413

site_idAC6
Number of Residues1
Detailsbinding site for residue ZN A 306
ChainResidue
APHE119

site_idAC7
Number of Residues3
Detailsbinding site for residue ZN A 307
ChainResidue
AASP81
ALYS112
AEPE302

site_idAC8
Number of Residues4
Detailsbinding site for residue ZN A 308
ChainResidue
ATRP79
ATHR142
AALA143
AASP175

site_idAC9
Number of Residues2
Detailsbinding site for residue ZN A 309
ChainResidue
ATRP205
BTRP205

site_idAD1
Number of Residues3
Detailsbinding site for residue NA A 310
ChainResidue
ATRP205
BPRO204
BTRP205

site_idAD2
Number of Residues8
Detailsbinding site for residue EPE B 301
ChainResidue
BTHR124
BGLU133
BTYR149
BLYS154
BARG191
BTYR192
BPRO193
BLYS194

site_idAD3
Number of Residues6
Detailsbinding site for residue ZN B 302
ChainResidue
BHIS78
BHIS80
BASP82
BHIS141
BZN303
BSO4312

site_idAD4
Number of Residues6
Detailsbinding site for residue ZN B 303
ChainResidue
BASP82
BCYS160
BHIS202
BZN302
BSO4312
BHOH405

site_idAD5
Number of Residues2
Detailsbinding site for residue ZN B 304
ChainResidue
ALYS179
BASP177

site_idAD6
Number of Residues4
Detailsbinding site for residue ZN B 305
ChainResidue
AASP116
BGLU42
BLYS72
BILE127

site_idAD7
Number of Residues2
Detailsbinding site for residue ZN B 306
ChainResidue
BGLY43
BGLN69

site_idAD8
Number of Residues4
Detailsbinding site for residue ZN B 307
ChainResidue
BGLU88
BGLN91
BARG92
BHOH406

site_idAD9
Number of Residues6
Detailsbinding site for residue ZN B 308
ChainResidue
BGLN130
BGLN131
BLEU150
BPRO151
BGLN152
BGLN153

site_idAE1
Number of Residues4
Detailsbinding site for residue ZN B 309
ChainResidue
BVAL162
BLYS163
BASP164
BHIS202

site_idAE2
Number of Residues1
Detailsbinding site for residue ZN B 311
ChainResidue
BPHE119

site_idAE3
Number of Residues3
Detailsbinding site for residue SO4 B 312
ChainResidue
BASP82
BZN302
BZN303

site_idAE4
Number of Residues2
Detailsbinding site for residue NA B 313
ChainResidue
BLEU102
BASP144

Functional Information from PROSITE/UniProt
site_idPS00744
Number of Residues13
DetailsBETA_LACTAMASE_B_2 Beta-lactamases class B signature 2. PqqkILfGgCLVK
ChainResidueDetails
APRO151-LYS163

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PDB entries from 2024-07-10

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