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3V7U

Crystal structure of NAD kinase 1 from Listeria monocytogenes in complex with MTA

Functional Information from GO Data
ChainGOidnamespacecontents
A0003951molecular_functionNAD+ kinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006741biological_processNADP biosynthetic process
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0019674biological_processNAD metabolic process
A0046872molecular_functionmetal ion binding
A0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE MTA A 301
ChainResidue
AASP45
AHOH429
AHOH450
AHOH470
AHOH484
APHE74
ATYR75
AASN122
ASER158
ATHR161
AALA162
AILE187
AMTA302

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE MTA A 302
ChainResidue
AGLY46
ALEU49
AASN122
AGLU123
AGLY149
AASP150
AALA162
ATYR163
ASER166
AALA185
AILE187
AMTA301
AHOH429
AHOH442

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE CIT A 303
ChainResidue
AVAL98
ATYR100
AHIS173
AARG247
APHE251
APRO252
APHE253
AARG256
AHOH434
AHOH454

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 304
ChainResidue
ALYS8
AGLY44
AGLY46
ATHR47

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:17686780
ChainResidueDetails
AASP45

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:17686780
ChainResidueDetails
AASP45
AGLY46
AASN122
ASER158
ATHR161
AHIS223

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00361
ChainResidueDetails
AARG148

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305|PubMed:17686780
ChainResidueDetails
AASP150

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PDB entries from 2024-08-28

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