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6U0Y

Crystal Structure of the metallo-beta-lactamase L1 from Stenotrophomonas maltophilia

Functional Information from GO Data
ChainGOidnamespacecontents
A0008270molecular_functionzinc ion binding
A0008800molecular_functionbeta-lactamase activity
A0017001biological_processantibiotic catabolic process
B0008270molecular_functionzinc ion binding
B0008800molecular_functionbeta-lactamase activity
B0017001biological_processantibiotic catabolic process
C0008270molecular_functionzinc ion binding
C0008800molecular_functionbeta-lactamase activity
C0017001biological_processantibiotic catabolic process
D0008270molecular_functionzinc ion binding
D0008800molecular_functionbeta-lactamase activity
D0017001biological_processantibiotic catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue ZN A 301
ChainResidue
AHIS105
AHIS107
AHIS181
AZN302
AEDO305

site_idAC2
Number of Residues5
Detailsbinding site for residue ZN A 302
ChainResidue
AEDO305
AASP109
AHIS110
AHIS246
AZN301

site_idAC3
Number of Residues7
Detailsbinding site for residue EDO A 303
ChainResidue
AARG137
AASN141
AHOH508
AHOH540
CALA156
CASP157
CHOH493

site_idAC4
Number of Residues4
Detailsbinding site for residue EDO A 304
ChainResidue
AALA172
ATHR191
AHOH433
AHOH449

site_idAC5
Number of Residues8
Detailsbinding site for residue EDO A 305
ChainResidue
ATYR32
AHIS105
AHIS107
AASP109
APHE145
AHIS181
AZN301
AZN302

site_idAC6
Number of Residues7
Detailsbinding site for residue ZN B 300
ChainResidue
BHIS105
BHIS107
BHIS181
BZN301
BEDO302
BHOH402
BHOH468

site_idAC7
Number of Residues7
Detailsbinding site for residue ZN B 301
ChainResidue
BASP109
BHIS110
BHIS246
BZN300
BEDO302
BHOH402
BHOH468

site_idAC8
Number of Residues8
Detailsbinding site for residue EDO B 302
ChainResidue
BHIS107
BASP109
BHIS181
BHIS246
BZN300
BZN301
BHOH402
BHOH468

site_idAC9
Number of Residues5
Detailsbinding site for residue EDO B 303
ChainResidue
BARG158
BVAL165
BVAL166
BTHR167
BHOH452

site_idAD1
Number of Residues7
Detailsbinding site for residue ZN C 301
ChainResidue
CHIS105
CHIS107
CHIS181
CZN302
CHOH406
CHOH560
CHOH568

site_idAD2
Number of Residues7
Detailsbinding site for residue ZN C 302
ChainResidue
CASP109
CHIS110
CHIS246
CZN301
CHOH406
CHOH560
CHOH562

site_idAD3
Number of Residues5
Detailsbinding site for residue EDO C 303
ChainResidue
CCYS239
CCYS267
CHOH441
CHOH510
CHOH512

site_idAD4
Number of Residues3
Detailsbinding site for residue EDO C 304
ChainResidue
CLEU90
CARG91
CHOH424

site_idAD5
Number of Residues5
Detailsbinding site for residue EDO C 305
ChainResidue
CLEU265
CTHR266
CALA269
CHOH515
CHOH539

site_idAD6
Number of Residues5
Detailsbinding site for residue ZN D 300
ChainResidue
DHIS105
DHIS107
DHIS181
DZN301
DEDO302

site_idAD7
Number of Residues5
Detailsbinding site for residue ZN D 301
ChainResidue
DASP109
DHIS110
DHIS246
DZN300
DEDO302

site_idAD8
Number of Residues7
Detailsbinding site for residue EDO D 302
ChainResidue
DZN301
DHIS105
DHIS107
DASP109
DPHE145
DHIS181
DZN300

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

219140

PDB entries from 2024-05-01

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