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5MM9

VIM-2_2b. Metallo-beta-Lactamase Inhibitors by Bioisosteric Replacement: Preparation, Activity and Binding

Functional Information from GO Data
ChainGOidnamespacecontents
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0046872molecular_functionmetal ion binding
B0016787molecular_functionhydrolase activity
B0017001biological_processantibiotic catabolic process
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue ZN A 401
ChainResidue
AHIS116
AHIS118
AHIS196
AZN402
A8SH404

site_idAC2
Number of Residues5
Detailsbinding site for residue ZN A 402
ChainResidue
A8SH404
AASP120
ACYS221
AHIS263
AZN401

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN A 403
ChainResidue
AHIS170
AHIS285
AHOH517
AHOH703

site_idAC4
Number of Residues12
Detailsbinding site for residue 8SH A 404
ChainResidue
APHE61
ATYR67
ATRP87
AHIS118
AASP120
AHIS196
AARG228
AASN233
AHIS263
AZN401
AZN402
AHOH640

site_idAC5
Number of Residues4
Detailsbinding site for residue ZN B 401
ChainResidue
BHIS116
BHIS118
BHIS196
B8SH405

site_idAC6
Number of Residues5
Detailsbinding site for residue ZN B 402
ChainResidue
BASP120
BARG121
BCYS221
BHIS263
B8SH405

site_idAC7
Number of Residues5
Detailsbinding site for residue MG B 403
ChainResidue
BTHR115
BHIS116
BGLY220
BCYS221
BHOH577

site_idAC8
Number of Residues4
Detailsbinding site for residue ZN B 404
ChainResidue
BHIS170
BHIS285
BHOH701
BHOH708

site_idAC9
Number of Residues13
Detailsbinding site for residue 8SH B 405
ChainResidue
AASP62
BPHE61
BTYR67
BTRP87
BHIS118
BASP119
BASP120
BHIS196
BARG228
BASN233
BHIS263
BZN401
BZN402

219140

PDB entries from 2024-05-01

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