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4RM5

Structural and mechanistic insights into NDM-1 catalyzed hydrolysis of cephalosporins

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
C0008270molecular_functionzinc ion binding
C0008800molecular_functionbeta-lactamase activity
C0016787molecular_functionhydrolase activity
C0017001biological_processantibiotic catabolic process
C0042597cellular_componentperiplasmic space
C0046677biological_processresponse to antibiotic
C0046872molecular_functionmetal ion binding
D0008270molecular_functionzinc ion binding
D0008800molecular_functionbeta-lactamase activity
D0016787molecular_functionhydrolase activity
D0017001biological_processantibiotic catabolic process
D0042597cellular_componentperiplasmic space
D0046677biological_processresponse to antibiotic
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 300
ChainResidue
AHIS120
AHIS122
AHIS189
AHOH401

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 301
ChainResidue
ACYS208
AHIS250
AHOH401
AHOH410

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 300
ChainResidue
BHIS122
BHIS189
BHOH401
BHOH539
BHIS120

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 301
ChainResidue
BCYS208
BHIS250
BHOH401
BHOH468

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 300
ChainResidue
CHIS120
CHIS122
CHIS189
CHOH401

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN C 301
ChainResidue
CASN124
CCYS208
CHIS250
CHOH401
CHOH518

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 300
ChainResidue
DHIS120
DHIS122
DHIS189
DHOH483

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 301
ChainResidue
DCYS208
DHIS250
DHOH426
DHOH483

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues24
DetailsBINDING: BINDING => ECO:0000269|PubMed:22713171, ECO:0000269|PubMed:25815530
ChainResidueDetails
AHIS120
BHIS189
BCYS208
BHIS250
CHIS120
CHIS122
CASN124
CHIS189
CCYS208
CHIS250
DHIS120
AHIS122
DHIS122
DASN124
DHIS189
DCYS208
DHIS250
AASN124
AHIS189
ACYS208
AHIS250
BHIS120
BHIS122
BASN124

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:22713171
ChainResidueDetails
ALYS211
AASN220
BLYS211
BASN220
CLYS211
CASN220
DLYS211
DASN220

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PDB entries from 2024-10-16

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