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4RAW

Crystal Structure of New Delhi Metallo-beta-Lactamase-1 Mutant M67V Complexed with Hydrolyzed Ampicillin

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 Residues20
DetailsBINDING SITE FOR RESIDUE ZZ7 A 301
ChainResidue
ALEU65
AASN220
AHIS250
ACD302
ACD303
AHOH439
AHOH453
AHOH570
AHOH585
BTHR34
BPRO68
ATRP93
BGLY69
AHIS122
AGLN123
AASP124
AHIS189
ACYS208
ALYS211
AGLY219

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CD A 302
ChainResidue
AHIS120
AHIS122
AHIS189
AZZ7301
AHOH570

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CD A 303
ChainResidue
AASP124
ACYS208
AHIS250
AZZ7301
AHOH570

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO A 304
ChainResidue
AASN110
AILE198
AASP199
ATHR201
AILE203
AALA243
AHOH435
AHOH595

site_idAC5
Number of Residues20
DetailsBINDING SITE FOR RESIDUE ZZ7 B 301
ChainResidue
ATHR34
APRO68
AGLY69
BLEU65
BTRP93
BHIS122
BGLN123
BASP124
BHIS189
BCYS208
BLYS211
BGLY219
BASN220
BHIS250
BCD302
BCD303
BHOH401
BHOH453
BHOH454
BHOH488

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CD B 302
ChainResidue
BHIS120
BHIS122
BHIS189
BZZ7301
BHOH401

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CD B 303
ChainResidue
BASP124
BCYS208
BHIS250
BZZ7301
BHOH401

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 2024-10-09

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