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4RL0

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
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 301
ChainResidue
AHIS120
AHIS122
AHIS189
A3S0303
AHOH426

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 302
ChainResidue
AHOH426
AASP124
ACYS208
AHIS250
A3S0303

site_idAC3
Number of Residues21
DetailsBINDING SITE FOR RESIDUE 3S0 A 303
ChainResidue
AILE35
ALEU65
ATRP93
AHIS122
AGLN123
AASP124
AGLU152
AHIS189
ACYS208
ALYS211
AGLY219
AASN220
AHIS250
AZN301
AZN302
AHOH426
AHOH563
BTHR34
BPRO68
BGLY69
BPHE70

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 301
ChainResidue
BHIS120
BHIS122
BHIS189
B3S0303
BHOH419

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 302
ChainResidue
BASP124
BCYS208
BHIS250
B3S0303
BHOH419

site_idAC6
Number of Residues19
DetailsBINDING SITE FOR RESIDUE 3S0 B 303
ChainResidue
ATHR34
APHE70
AHOH529
BILE35
BLEU65
BTRP93
BHIS122
BGLN123
BASP124
BHIS189
BCYS208
BLYS211
BGLY219
BASN220
BHIS250
BZN301
BZN302
BHOH419
BHOH592

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

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PDB entries from 2024-08-14

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