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6V73

Crystal Structure of Metallo Beta Lactamase from Erythrobacter litoralis with beta mercaptoethanol in the active site

Functional Information from GO Data
ChainGOidnamespacecontents
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 301
ChainResidue
AHIS112
AHIS114
AHIS181
AZN302
ABME304

site_idAC2
Number of Residues5
Detailsbinding site for residue ZN A 302
ChainResidue
ABME304
AASP116
ACYS200
AHIS242
AZN301

site_idAC3
Number of Residues4
Detailsbinding site for residue CL A 303
ChainResidue
APHE232
APRO233
AASP234
AALA235

site_idAC4
Number of Residues7
Detailsbinding site for residue BME A 304
ChainResidue
AHIS114
AASP116
AHIS181
ACYS200
AASN212
AZN301
AZN302

site_idAC5
Number of Residues8
Detailsbinding site for residue FMT A 305
ChainResidue
APHE62
APHE62
AILE65
AILE65
AHOH414
AHOH414
AHOH415
AHOH415

Functional Information from PROSITE/UniProt
site_idPS00014
Number of Residues4
DetailsER_TARGET Endoplasmic reticulum targeting sequence. AEEL
ChainResidueDetails
AALA258-LEU261

249697

PDB entries from 2026-02-25

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