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5DPX

1,2,4-Triazole-3-thione compounds as inhibitors of L1, di-zinc metallo-beta-lactamases.

Functional Information from GO Data
ChainGOidnamespacecontents
A0008270molecular_functionzinc ion binding
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0030655biological_processbeta-lactam antibiotic 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
B0030655biological_processbeta-lactam antibiotic catabolic process
B0042597cellular_componentperiplasmic space
B0046677biological_processresponse to antibiotic
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 401
ChainResidue
AHIS105
AHIS107
AHIS181
AL3B403

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN A 402
ChainResidue
AASP109
AHIS110
AHIS246
AL3B403

site_idAC3
Number of Residues15
Detailsbinding site for residue L3B A 403
ChainResidue
AHIS107
AASP109
AHIS110
AASP142
APHE145
AILE149
AHIS181
ASER206
ATYR212
AHIS246
AZN401
AZN402
AHOH542
AHOH582
ATYR32

site_idAC4
Number of Residues9
Detailsbinding site for residue SO4 A 404
ChainResidue
AALA258
AARG259
AALA260
AGLY261
AALA262
AHOH559
AHOH563
BARG235
BLYS268

site_idAC5
Number of Residues4
Detailsbinding site for residue SO4 A 405
ChainResidue
AARG158
AILE166
ATHR167
AHOH575

site_idAC6
Number of Residues4
Detailsbinding site for residue SO4 A 406
ChainResidue
ATRP52
AARG91
AHOH515
AHOH553

site_idAC7
Number of Residues4
Detailsbinding site for residue ZN B 401
ChainResidue
BHIS105
BHIS107
BHIS181
BL3B403

site_idAC8
Number of Residues4
Detailsbinding site for residue ZN B 402
ChainResidue
BASP109
BHIS110
BHIS246
BL3B403

site_idAC9
Number of Residues14
Detailsbinding site for residue L3B B 403
ChainResidue
BTYR32
BHIS105
BHIS107
BASP109
BHIS110
BPHE145
BILE149
BHIS181
BSER206
BTYR212
BHIS246
BZN401
BZN402
BHOH505

site_idAD1
Number of Residues6
Detailsbinding site for residue SO4 B 404
ChainResidue
BARG158
BILE166
BTHR167
BHOH538
BHOH612
BHOH644

Functional Information from PROSITE/UniProt
site_idPS00743
Number of Residues21
DetailsBETA_LACTAMASE_B_1 Beta-lactamases class B signature 1. LlSHaHADhaGPvaelkrrtG
ChainResidueDetails
ALEU102-GLY122

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:17999929, ECO:0000269|PubMed:9811546
ChainResidueDetails
AHIS105
BHIS181
AHIS107
AASP109
AHIS110
AHIS181
BHIS105
BHIS107
BASP109
BHIS110

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P25910
ChainResidueDetails
AASP205
BASP205

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:9811546
ChainResidueDetails
AHIS246
BHIS246

Catalytic Information from CSA
site_idMCSA1
Number of Residues7
DetailsM-CSA 258
ChainResidueDetails
AHIS105metal ligand
AHIS107metal ligand
AASP109metal ligand
AHIS110metal ligand
AHIS181metal ligand
ATYR212electrostatic stabiliser, hydrogen bond donor
AHIS246metal ligand

site_idMCSA2
Number of Residues7
DetailsM-CSA 258
ChainResidueDetails
BHIS105metal ligand
BHIS107metal ligand
BASP109metal ligand
BHIS110metal ligand
BHIS181metal ligand
BTYR212electrostatic stabiliser, hydrogen bond donor
BHIS246metal ligand

218853

PDB entries from 2024-04-24

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