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5HH5

Crystal structure of B3 metallo-beta-lactamase L1 complexed with a phosphonate-based 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
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue ZN A 401
ChainResidue
AHIS116
AHIS118
AHIS196
A60M407
AHOH501

site_idAC2
Number of Residues5
Detailsbinding site for residue SO4 A 402
ChainResidue
AHOH606
AARG172
AVAL179
AILE180
ATHR181

site_idAC3
Number of Residues4
Detailsbinding site for residue SO4 A 403
ChainResidue
ATRP53
AARG102
AHOH523
AHOH530

site_idAC4
Number of Residues9
Detailsbinding site for residue SO4 A 404
ChainResidue
AARG209
AARG252
AALA275
AARG276
AALA289
AGLY290
AALA291
ALYS297
AHOH541

site_idAC5
Number of Residues2
Detailsbinding site for residue SO4 A 405
ChainResidue
AARG209
AARG252

site_idAC6
Number of Residues8
Detailsbinding site for residue GOL A 406
ChainResidue
AARG130
AARG148
AASP152
AASP171
AARG172
AILE173
AHOH537
AHOH621

site_idAC7
Number of Residues14
Detailsbinding site for residue 60M A 407
ChainResidue
AHIS116
AHIS118
AASP120
AHIS121
AHIS196
ASER221
ASER225
AHIS263
AALA266
AZN401
AHOH501
AHOH511
AHOH578
AHOH626

Functional Information from PROSITE/UniProt
site_idPS00743
Number of Residues21
DetailsBETA_LACTAMASE_B_1 Beta-lactamases class B signature 1. LlSHaHADhaGPvaelkrrtG
ChainResidueDetails
ALEU113-GLY133

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:17999929, ECO:0000269|PubMed:9811546
ChainResidueDetails
AHIS116
AHIS118
AASP120
AHIS121
AHIS196

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P25910
ChainResidueDetails
AASP220

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:9811546
ChainResidueDetails
AHIS263

Catalytic Information from CSA
site_idMCSA1
Number of Residues7
DetailsM-CSA 258
ChainResidueDetails
AHIS116metal ligand
AHIS118metal ligand
AASP120metal ligand
AHIS121metal ligand
AHIS196metal ligand
ATYR229electrostatic stabiliser, hydrogen bond donor
AHIS263metal ligand

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PDB entries from 2024-07-24

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