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5NDB

Crystal structure of metallo-beta-lactamase SPM-1 complexed with cyclobutanone inhibitor

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 Residues6
Detailsbinding site for residue ZN A 401
ChainResidue
AASP110
ACYS220
AHIS262
AZN402
A8TW412
AHOH532

site_idAC2
Number of Residues6
Detailsbinding site for residue ZN A 402
ChainResidue
AZN401
A8TW412
AHOH532
AHIS106
AHIS108
AHIS195

site_idAC3
Number of Residues1
Detailsbinding site for residue GOL A 403
ChainResidue
ALYS151

site_idAC4
Number of Residues4
Detailsbinding site for residue GOL A 404
ChainResidue
AARG135
AGLU138
AARG143
AALA147

site_idAC5
Number of Residues1
Detailsbinding site for residue GOL A 405
ChainResidue
AMET121

site_idAC6
Number of Residues2
Detailsbinding site for residue GOL A 406
ChainResidue
A8TW412
AHOH514

site_idAC7
Number of Residues4
Detailsbinding site for residue ZN A 407
ChainResidue
AHIS33
AASP35
BGLU116
BHIS163

site_idAC8
Number of Residues7
Detailsbinding site for residue DMS A 408
ChainResidue
AASP35
ALEU36
APRO37
BASN81
BGLN85
BLYS120
BHOH562

site_idAC9
Number of Residues3
Detailsbinding site for residue CL A 410
ChainResidue
AVAL178
AHOH562
AHOH568

site_idAD1
Number of Residues1
Detailsbinding site for residue CL A 411
ChainResidue
AHOH591

site_idAD2
Number of Residues13
Detailsbinding site for residue 8TW A 412
ChainResidue
ATYR59
APHE79
AASP110
AHIS195
ACYS220
ALYS223
ATYR232
AHIS262
AZN401
AZN402
AGOL406
AHOH532
AHOH577

site_idAD3
Number of Residues6
Detailsbinding site for residue ZN B 401
ChainResidue
BASP110
BCYS220
BHIS262
BZN402
B8TW409
BHOH506

site_idAD4
Number of Residues6
Detailsbinding site for residue ZN B 402
ChainResidue
BHIS106
BHIS108
BHIS195
BZN401
B8TW409
BHOH506

site_idAD5
Number of Residues2
Detailsbinding site for residue GOL B 403
ChainResidue
BTYR59
B8TW409

site_idAD6
Number of Residues3
Detailsbinding site for residue GOL B 405
ChainResidue
BPRO97
BLYS98
BMET121

site_idAD7
Number of Residues4
Detailsbinding site for residue ZN B 406
ChainResidue
AGLU116
AHIS163
BHIS33
BASP35

site_idAD8
Number of Residues12
Detailsbinding site for residue 8TW B 409
ChainResidue
BTYR59
BPHE79
BASP110
BHIS195
BCYS220
BLYS223
BTYR232
BHIS262
BZN401
BZN402
BGOL403
BHOH506

site_idAD9
Number of Residues3
Detailsbinding site for residue SO4 B 410
ChainResidue
BARG157
BSER161
BHOH507

site_idAE1
Number of Residues3
Detailsbinding site for residue TRS B 411
ChainResidue
ALEU230
AGLU312
BASP235

Functional Information from PROSITE/UniProt
site_idPS00744
Number of Residues13
DetailsBETA_LACTAMASE_B_2 Beta-lactamases class B signature 2. PkkkLLfGgCMIK
ChainResidueDetails
APRO205-LYS223

221051

PDB entries from 2024-06-12

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