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6OFB

Crystal structure of human glutamine-dependent NAD+ synthetase complexed with NaAD+, AMP, pyrophosphate, and Mg2+

Functional Information from GO Data
ChainGOidnamespacecontents
A0003952molecular_functionNAD+ synthase (glutamine-hydrolyzing) activity
A0004359molecular_functionglutaminase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0009435biological_processNAD biosynthetic process
A0016874molecular_functionligase activity
A0034627biological_process'de novo' NAD biosynthetic process
B0003952molecular_functionNAD+ synthase (glutamine-hydrolyzing) activity
B0004359molecular_functionglutaminase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0009435biological_processNAD biosynthetic process
B0016874molecular_functionligase activity
B0034627biological_process'de novo' NAD biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues13
Detailsbinding site for residue DND A 901
ChainResidue
AASN483
BGLN349
BGLN498
BLEU510
BASP535
AARG487
ALEU526
ATHR527
ALYS528
AASP590
AHIS648
ALYS649
AAMP902

site_idAC2
Number of Residues10
Detailsbinding site for residue AMP A 902
ChainResidue
APRO355
ALEU356
ASER357
ACYS416
AMET418
AARG489
ACYS531
AALA573
ADND901
APOP903

site_idAC3
Number of Residues7
Detailsbinding site for residue POP A 903
ChainResidue
ASER357
AGLY359
AASP361
ASER362
AAMP902
AMG904
ACL909

site_idAC4
Number of Residues6
Detailsbinding site for residue MG A 904
ChainResidue
AGLY359
AVAL360
AASP361
ALYS544
APOP903
ACL909

site_idAC5
Number of Residues1
Detailsbinding site for residue CL A 905
ChainResidue
AARG145

site_idAC6
Number of Residues1
Detailsbinding site for residue CL A 906
ChainResidue
BARG93

site_idAC7
Number of Residues1
Detailsbinding site for residue CL A 907
ChainResidue
AARG476

site_idAC8
Number of Residues5
Detailsbinding site for residue CL A 908
ChainResidue
AVAL360
ALYS544
AARG548
AALA571
ACL909

site_idAC9
Number of Residues5
Detailsbinding site for residue CL A 909
ChainResidue
AVAL360
AALA571
APOP903
AMG904
ACL908

site_idAD1
Number of Residues19
Detailsbinding site for residue DND B 901
ChainResidue
AGLN349
AGLN498
ALEU510
ALEU511
AASP535
BLEU479
BGLN482
BASN483
BARG487
BLEU526
BTHR527
BLYS528
BASP530
BLEU575
BASP590
BHIS648
BLYS649
BPHE674
BAMP902

site_idAD2
Number of Residues10
Detailsbinding site for residue AMP B 902
ChainResidue
BPRO355
BLEU356
BSER357
BCYS416
BMET418
BARG489
BALA573
BLEU575
BDND901
BPOP903

site_idAD3
Number of Residues8
Detailsbinding site for residue POP B 903
ChainResidue
BSER357
BGLY359
BASP361
BSER362
BLYS544
BAMP902
BMG904
BCL908

site_idAD4
Number of Residues6
Detailsbinding site for residue MG B 904
ChainResidue
BGLY359
BVAL360
BASP361
BLYS544
BPOP903
BCL908

site_idAD5
Number of Residues1
Detailsbinding site for residue CL B 905
ChainResidue
BARG476

site_idAD6
Number of Residues2
Detailsbinding site for residue CL B 906
ChainResidue
ASER475
BSER475

site_idAD7
Number of Residues3
Detailsbinding site for residue CL B 907
ChainResidue
BARG548
BALA571
BCL908

site_idAD8
Number of Residues5
Detailsbinding site for residue CL B 908
ChainResidue
BALA571
BPOP903
BMG904
BCL907
BVAL360

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor; for glutaminase activity => ECO:0000250|UniProtKB:P9WJJ3
ChainResidueDetails
AGLU45
BGLU45

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: For glutaminase activity => ECO:0000250|UniProtKB:P9WJJ3
ChainResidueDetails
ALYS114
BLYS114

site_idSWS_FT_FI3
Number of Residues2
DetailsACT_SITE: Nucleophile; for glutaminase activity => ECO:0000250|UniProtKB:P9WJJ3
ChainResidueDetails
ACYS175
BCYS175

site_idSWS_FT_FI4
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
ASER357
BSER357

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
APRO355
BPRO355

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PDB entries from 2024-07-17

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