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5DHP

Crystal structure of NAD kinase 1 from Listeria monocytogenes in complex with a novel inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0003951molecular_functionNAD+ kinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006741biological_processNADP biosynthetic process
A0016301molecular_functionkinase activity
A0019674biological_processNAD metabolic process
A0046872molecular_functionmetal ion binding
A0051287molecular_functionNAD binding
B0003951molecular_functionNAD+ kinase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006741biological_processNADP biosynthetic process
B0016301molecular_functionkinase activity
B0019674biological_processNAD metabolic process
B0046872molecular_functionmetal ion binding
B0051287molecular_functionNAD binding
C0003951molecular_functionNAD+ kinase activity
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0006741biological_processNADP biosynthetic process
C0016301molecular_functionkinase activity
C0019674biological_processNAD metabolic process
C0046872molecular_functionmetal ion binding
C0051287molecular_functionNAD binding
D0003951molecular_functionNAD+ kinase activity
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0006741biological_processNADP biosynthetic process
D0016301molecular_functionkinase activity
D0019674biological_processNAD metabolic process
D0046872molecular_functionmetal ion binding
D0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue CIT A 301
ChainResidue
AVAL98
ATYR100
AHIS173
APHE251
APRO252
APHE253
AARG256
AHOH401
AHOH404

site_idAC2
Number of Residues4
Detailsbinding site for residue GOL A 302
ChainResidue
ALYS127
AASP150
AMET184
CASP150

site_idAC3
Number of Residues12
Detailsbinding site for residue 5AQ A 303
ChainResidue
AASN122
AGLU123
AALA162
ATYR163
ASER166
AHIS223
AHOH468
CGLY131
CPRO132
CGLY149
CASP150
CALA185

site_idAC4
Number of Residues11
Detailsbinding site for residue CIT B 301
ChainResidue
BVAL98
BTYR100
BHIS173
BARG247
BPRO252
BPHE253
BARG256
BHOH401
BHOH404
BHOH407
BHOH431

site_idAC5
Number of Residues14
Detailsbinding site for residue 5AQ B 302
ChainResidue
BASN122
BGLU123
BALA162
BTYR163
BSER166
BASP222
BHIS223
BHOH433
DGLY131
DPRO132
DGLY149
DASP150
DALA185
DILE187

site_idAC6
Number of Residues14
Detailsbinding site for residue 5AQ C 301
ChainResidue
AGLY131
APRO132
AGLY149
AASP150
AALA185
CASN122
CGLU123
CALA162
CTYR163
CSER166
CASP222
CHOH437
CHOH438
CHOH447

site_idAC7
Number of Residues6
Detailsbinding site for residue CIT D 301
ChainResidue
DTYR100
DHIS173
DARG247
DPHE251
DPRO252
DPHE253

site_idAC8
Number of Residues10
Detailsbinding site for residue 5AQ D 302
ChainResidue
BARG148
BASP150
BALA185
BILE187
DASN122
DGLU123
DALA162
DTYR163
DSER166
DHIS223

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:17686780
ChainResidueDetails
AASP45
BASP45
CASP45
DASP45

site_idSWS_FT_FI2
Number of Residues24
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:17686780
ChainResidueDetails
ATHR161
AHIS223
BASP45
BGLY46
BASN122
BSER158
BTHR161
BHIS223
CASP45
CGLY46
CASN122
CSER158
CTHR161
CHIS223
DASP45
DGLY46
DASN122
DSER158
DTHR161
DHIS223
AASP45
AGLY46
AASN122
ASER158

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00361
ChainResidueDetails
AARG148
BARG148
CARG148
DARG148

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305|PubMed:17686780
ChainResidueDetails
AASP150
BASP150
CASP150
DASP150

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PDB entries from 2024-06-12

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