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

6MGZ

Crystal Structure of the New Deli Metallo Beta Lactamase Variant 4 from Klebsiella pneumoniae

Functional Information from GO Data
ChainGOidnamespacecontents
A0008270molecular_functionzinc ion binding
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0042597cellular_componentperiplasmic space
A0046677biological_processresponse to antibiotic
A0046872molecular_functionmetal ion binding
B0008270molecular_functionzinc ion binding
B0008800molecular_functionbeta-lactamase activity
B0016787molecular_functionhydrolase activity
B0017001biological_processantibiotic catabolic process
B0042597cellular_componentperiplasmic space
B0046677biological_processresponse to antibiotic
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 300
ChainResidue
AHIS120
AHIS122
AHIS189
AHOH432

site_idAC2
Number of Residues6
Detailsbinding site for residue ZN A 301
ChainResidue
BHOH412
AASP124
ACYS208
AHIS250
AFMT306
AHOH432

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN A 302
ChainResidue
AGLU152
AASP223
AFMT303
BGLU227

site_idAC4
Number of Residues6
Detailsbinding site for residue FMT A 303
ChainResidue
AHIS122
AGLU152
AASP223
AZN302
AHOH494
BGLU227

site_idAC5
Number of Residues1
Detailsbinding site for residue FMT A 304
ChainResidue
AHOH405

site_idAC6
Number of Residues4
Detailsbinding site for residue FMT A 305
ChainResidue
APRO112
AVAL113
AHOH413
AHOH499

site_idAC7
Number of Residues8
Detailsbinding site for residue FMT A 306
ChainResidue
AHIS189
ACYS208
ALYS211
AGLY219
AASN220
AHIS250
AZN301
BGLY69

site_idAC8
Number of Residues6
Detailsbinding site for residue ZN B 300
ChainResidue
BHIS120
BHIS122
BHIS189
BZN301
BHOH420
BHOH454

site_idAC9
Number of Residues6
Detailsbinding site for residue ZN B 301
ChainResidue
BASP124
BCYS208
BHIS250
BZN300
BFMT305
BHOH420

site_idAD1
Number of Residues4
Detailsbinding site for residue ZN B 302
ChainResidue
AGLU227
BGLU152
BASP223
BFMT303

site_idAD2
Number of Residues4
Detailsbinding site for residue FMT B 303
ChainResidue
AGLU227
BGLU152
BASP223
BZN302

site_idAD3
Number of Residues5
Detailsbinding site for residue MG B 304
ChainResidue
BASP95
BASP130
BHOH418
BHOH487
BHOH492

site_idAD4
Number of Residues7
Detailsbinding site for residue FMT B 305
ChainResidue
BHIS189
BCYS208
BLYS211
BGLY219
BASN220
BHIS250
BZN301

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:22713171, ECO:0000269|PubMed:25815530
ChainResidueDetails
AHIS120
BHIS189
BCYS208
BHIS250
AHIS122
AASP124
AHIS189
ACYS208
AHIS250
BHIS120
BHIS122
BASP124

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:22713171
ChainResidueDetails
ALYS211
AASN220
BLYS211
BASN220

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon