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5O2F

Crystal structure of NDM-1 in complex with hydrolyzed ampicillin - new refinement

Replaces:  4RL2
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
AZZ7303
AHOH443

site_idAC2
Number of Residues5
Detailsbinding site for residue ZN A 302
ChainResidue
AHOH443
AASP124
ACYS208
AHIS250
AZZ7303

site_idAC3
Number of Residues20
Detailsbinding site for residue ZZ7 A 303
ChainResidue
ATRP93
AHIS122
AGLN123
AASP124
AHIS189
ACYS208
ALYS211
AGLY219
AASN220
AHIS250
AZN301
AZN302
AHOH443
AHOH488
AHOH491
AHOH511
BTHR34
BPRO68
BGLY69
BPHE70

site_idAC4
Number of Residues2
Detailsbinding site for residue SO4 A 304
ChainResidue
AARG234
AARG264

site_idAC5
Number of Residues3
Detailsbinding site for residue SO4 A 305
ChainResidue
AHIS261
AARG264
AHOH481

site_idAC6
Number of Residues5
Detailsbinding site for residue SO4 A 306
ChainResidue
AARG270
AHOH486
BARG264
BLYS268
BHOH401

site_idAC7
Number of Residues1
Detailsbinding site for residue CL A 307
ChainResidue
AGLY29

site_idAC8
Number of Residues5
Detailsbinding site for residue EDO A 308
ChainResidue
ALYS216
ASER217
AHOH472
AHOH514
BLYS216

site_idAC9
Number of Residues3
Detailsbinding site for residue EDO A 309
ChainResidue
AHIS159
ASER160
AGLY178

site_idAD1
Number of Residues5
Detailsbinding site for residue ZN B 301
ChainResidue
BHIS120
BHIS122
BHIS189
BZZ7303
BHOH423

site_idAD2
Number of Residues5
Detailsbinding site for residue ZN B 302
ChainResidue
BASP124
BCYS208
BHIS250
BZZ7303
BHOH423

site_idAD3
Number of Residues20
Detailsbinding site for residue ZZ7 B 303
ChainResidue
ATHR34
APRO68
AGLY69
BLEU65
BTRP93
BHIS122
BGLN123
BASP124
BHIS189
BCYS208
BLYS211
BGLY219
BASN220
BHIS250
BZN301
BZN302
BHOH423
BHOH505
BHOH507
BHOH535

site_idAD4
Number of Residues8
Detailsbinding site for residue SO4 B 304
ChainResidue
BPRO150
BGLY153
BHIS261
BARG264
BHOH406
BHOH427
BHOH490
BHOH491

site_idAD5
Number of Residues2
Detailsbinding site for residue EDO B 305
ChainResidue
BHIS159
BSER160

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

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

221051

PDB entries from 2024-06-12

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