Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6U10

Crystal Structure of the metallo-beta-lactamase L1 from Stenotrophomonas maltophilia in the complex with the inhibitor captopril

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 Residues5
Detailsbinding site for residue ZN A 301
ChainResidue
AASP109
AHIS110
AHIS246
AX8Z303
AFMT304

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN A 302
ChainResidue
AHIS105
AHIS107
AHIS181
AX8Z303

site_idAC3
Number of Residues13
Detailsbinding site for residue X8Z A 303
ChainResidue
ATYR32
ATRP38
AHIS105
AASP109
APHE145
AILE149
AHIS181
APRO210
AHIS246
AZN301
AZN302
AFMT304
AHOH430

site_idAC4
Number of Residues7
Detailsbinding site for residue FMT A 304
ChainResidue
AHIS181
ASER206
ASER208
AHIS246
AZN301
AX8Z303
AHOH401

site_idAC5
Number of Residues11
Detailsbinding site for residue X8Z A 305
ChainResidue
AARG119
AALA136
AARG137
AALA154
ASER155
AALA156
AILE159
AFMT309
AHOH464
AHOH529
AHOH548

site_idAC6
Number of Residues4
Detailsbinding site for residue FMT A 306
ChainResidue
AVAL47
AALA48
AARG194
AHOH411

site_idAC7
Number of Residues4
Detailsbinding site for residue EDO A 307
ChainResidue
AARG200
AHOH432
AHOH477
AHOH525

site_idAC8
Number of Residues3
Detailsbinding site for residue FMT A 308
ChainResidue
AARG194
AASP240
AHOH585

site_idAC9
Number of Residues7
Detailsbinding site for residue FMT A 309
ChainResidue
AALA132
AALA136
AALA154
ASER155
AALA156
AX8Z305
AHOH611

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

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon