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6U2Z

Crystal Structure of the metallo-beta-lactamase L1 from Stenotrophomonas maltophilia in the complex with the hydrolyzed moxalactam and two copper ions

Functional Information from GO Data
ChainGOidnamespacecontents
A0008270molecular_functionzinc ion binding
A0008800molecular_functionbeta-lactamase activity
A0017001biological_processantibiotic catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue 3P7 A 300
ChainResidue
ATYR32
AHIS246
ACU301
ACU302
AHOH409
AHOH416
AHIS107
AASP109
AHIS110
APHE145
AHIS181
ASER206
ASER208
APRO210

site_idAC2
Number of Residues6
Detailsbinding site for residue CU A 301
ChainResidue
AASP109
AHIS110
AHIS246
A3P7300
ACU302
AHOH416

site_idAC3
Number of Residues6
Detailsbinding site for residue CU A 302
ChainResidue
AHIS105
AHIS107
AHIS181
A3P7300
ACU301
AHOH416

site_idAC4
Number of Residues8
Detailsbinding site for residue EDO A 303
ChainResidue
AASP142
ALEU143
AHIS181
ATHR182
APRO183
AHOH415
AHOH420
AHOH443

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

222624

PDB entries from 2024-07-17

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