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5NDE

Crystal structure of metallo-beta-lactamase SPM-1 in space group P4222

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 401
ChainResidue
AHIS35
AASP37
AHOH501
BGLU118
BHIS165

site_idAC2
Number of Residues5
Detailsbinding site for residue ZN A 402
ChainResidue
AGOL411
AHIS108
AHIS110
AHIS197
AZN403

site_idAC3
Number of Residues5
Detailsbinding site for residue ZN A 403
ChainResidue
AASP112
ACYS222
AHIS264
AZN402
AGOL411

site_idAC4
Number of Residues4
Detailsbinding site for residue ZN A 404
ChainResidue
AGLU118
AHIS165
BHIS35
BASP37

site_idAC5
Number of Residues6
Detailsbinding site for residue SO4 A 405
ChainResidue
ALYS208
AARG248
AHOH508
AHOH532
AHOH533
AHOH631

site_idAC6
Number of Residues7
Detailsbinding site for residue SO4 A 406
ChainResidue
ALYS179
AVAL180
AARG249
AHOH522
AHOH535
AHOH561
AHOH599

site_idAC7
Number of Residues5
Detailsbinding site for residue SO4 A 407
ChainResidue
ALYS251
AASN302
AHOH502
AHOH507
AHOH633

site_idAC8
Number of Residues10
Detailsbinding site for residue GOL A 408
ChainResidue
AASP37
ALEU38
APRO39
AHOH512
AHOH625
AHOH647
AHOH680
BASN83
BGLN87
BLYS122

site_idAC9
Number of Residues9
Detailsbinding site for residue GOL A 409
ChainResidue
AALA311
AMET315
AHOH564
AHOH600
BPRO195
BPRO199
BASN239
BHOH519
BHOH592

site_idAD1
Number of Residues5
Detailsbinding site for residue GOL A 410
ChainResidue
AHIS110
ATYR234
AGOL411
AHOH511
AHOH514

site_idAD2
Number of Residues9
Detailsbinding site for residue GOL A 411
ChainResidue
AHIS197
ACYS222
ALYS225
AGLY233
ATYR234
AHIS264
AZN402
AZN403
AGOL410

site_idAD3
Number of Residues2
Detailsbinding site for residue CL A 412
ChainResidue
AASN302
ALYS306

site_idAD4
Number of Residues1
Detailsbinding site for residue CL A 413
ChainResidue
AASP144

site_idAD5
Number of Residues5
Detailsbinding site for residue ZN B 401
ChainResidue
BHIS108
BHIS110
BHIS197
BZN402
BHOH638

site_idAD6
Number of Residues6
Detailsbinding site for residue ZN B 402
ChainResidue
BASP112
BCYS222
BHIS264
BZN401
BGOL404
BHOH638

site_idAD7
Number of Residues3
Detailsbinding site for residue SO4 B 403
ChainResidue
BLYS143
BASP144
BHOH503

site_idAD8
Number of Residues9
Detailsbinding site for residue GOL B 404
ChainResidue
BHIS197
BCYS222
BLYS225
BTYR234
BHIS264
BZN402
BHOH561
BHOH634
BHOH638

Functional Information from PROSITE/UniProt
site_idPS00744
Number of Residues13
DetailsBETA_LACTAMASE_B_2 Beta-lactamases class B signature 2. PkkkLLfGgCMIK
ChainResidueDetails
APRO207-LYS225

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PDB entries from 2024-06-12

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