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

5N0I

Crystal structure of NDM-1 in complex with beta-mercaptoethanol - new refinement

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
AASP124
ACYS208
AHIS250
AZN302
ABME303

site_idAC2
Number of Residues5
Detailsbinding site for residue ZN A 302
ChainResidue
ABME303
AHIS120
AHIS122
AHIS189
AZN301

site_idAC3
Number of Residues7
Detailsbinding site for residue BME A 303
ChainResidue
AHIS122
AASP124
AHIS189
AASN220
AZN301
AZN302
AHOH529

site_idAC4
Number of Residues7
Detailsbinding site for residue GOL A 304
ChainResidue
AARG81
AILE109
AHOH419
AHOH425
BARG52
BGLN53
BLEU54

site_idAC5
Number of Residues7
Detailsbinding site for residue GOL A 305
ChainResidue
ALYS106
AASN110
ALEU111
AHOH431
AHOH521
BGLU40
BTHR41

site_idAC6
Number of Residues5
Detailsbinding site for residue ZN B 301
ChainResidue
BASP124
BCYS208
BHIS250
BZN302
BBME303

site_idAC7
Number of Residues5
Detailsbinding site for residue ZN B 302
ChainResidue
BHIS120
BHIS122
BHIS189
BZN301
BBME303

site_idAC8
Number of Residues7
Detailsbinding site for residue BME B 303
ChainResidue
BHIS122
BASP124
BHIS189
BZN301
BZN302
BGOL304
BHOH532

site_idAC9
Number of Residues8
Detailsbinding site for residue GOL B 304
ChainResidue
BHIS122
BGLY219
BASN220
BLEU221
BBME303
BHOH401
BHOH408
BHOH491

site_idAD1
Number of Residues5
Detailsbinding site for residue CL B 305
ChainResidue
BPHE240
BPRO241
BLYS242
BALA243
BHOH613

site_idAD2
Number of Residues4
Detailsbinding site for residue PG4 B 306
ChainResidue
BLEU65
BASP66
BHOH500
BHOH583

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

224004

PDB entries from 2024-08-21

PDB statisticsPDBj update infoContact PDBjnumon