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6UAH

Crystal Structure of the Metallo-beta-Lactamase L1 from Stenotrophomonas maltophilia in the Complex with Hydrolyzed Meropenem

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 Residues4
Detailsbinding site for residue ZN A 301
ChainResidue
AHIS105
AHIS107
AHIS181
ALMP303

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN A 302
ChainResidue
AASP109
AHIS110
AHIS246
ALMP303

site_idAC3
Number of Residues15
Detailsbinding site for residue LMP A 303
ChainResidue
AHIS105
AHIS107
AASP109
AHIS110
APHE145
AHIS181
ASER206
ASER208
APRO210
AHIS246
ALYS277
AZN301
AZN302
AHOH479
ATYR32

site_idAC4
Number of Residues4
Detailsbinding site for residue PGE A 304
ChainResidue
AALA249
AALA273
ALYS277
AEDO305

site_idAC5
Number of Residues6
Detailsbinding site for residue EDO A 305
ChainResidue
AALA209
APRO210
ALYS277
AGLN281
APGE304
AHOH402

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

222415

PDB entries from 2024-07-10

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