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6TNH

Deoxyguanylosuccinate synthase (DgsS) quaternary structure with AMPPcP, dGMP, Asp, Magnesium at 2.21 Angstrom resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0004019molecular_functionadenylosuccinate synthase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006164biological_processpurine nucleotide biosynthetic process
A0016874molecular_functionligase activity
A0044208biological_process'de novo' AMP biosynthetic process
A0046040biological_processIMP metabolic process
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0004019molecular_functionadenylosuccinate synthase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006164biological_processpurine nucleotide biosynthetic process
B0016874molecular_functionligase activity
B0044208biological_process'de novo' AMP biosynthetic process
B0046040biological_processIMP metabolic process
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue SO4 A 401
ChainResidue
AASN28
AARG180
ALYS224
ALYS325

site_idAC2
Number of Residues5
Detailsbinding site for residue SO4 A 402
ChainResidue
ALYS68
AARG69
AALA177
AHOH539
AHOH541

site_idAC3
Number of Residues3
Detailsbinding site for residue SO4 A 403
ChainResidue
ASER79
AARG82
AHOH563

site_idAC4
Number of Residues3
Detailsbinding site for residue SO4 A 404
ChainResidue
AASN81
AHOH526
AHOH552

site_idAC5
Number of Residues22
Detailsbinding site for residue DGP A 405
ChainResidue
APHE12
ASER14
AASN40
AALA41
AILE125
AGLY126
ASER127
ATHR128
AGLN187
ALEU191
ACYS201
ATHR202
AVAL236
ASER240
AACP406
AHOH509
AHOH514
AHOH515
AHOH531
AHOH553
AHOH625
BARG142

site_idAC6
Number of Residues21
Detailsbinding site for residue ACP A 406
ChainResidue
AGLY13
ASER14
ATHR15
AGLY16
ALYS17
AGLY18
AALA41
AGLY42
AHIS43
ATHR44
AGLN187
AASN294
APHE295
AASN297
AGLY330
APRO331
ADGP405
AHOH504
AHOH523
AHOH543
AHOH565

site_idAC7
Number of Residues5
Detailsbinding site for residue ASP A 407
ChainResidue
ATHR262
ATHR263
AVAL264
AARG269
AHOH523

site_idAC8
Number of Residues22
Detailsbinding site for residue DGP B 401
ChainResidue
AARG142
BPHE12
BGLY13
BSER14
BASN40
BALA41
BGLY126
BSER127
BTHR128
BGLN187
BLEU191
BCYS201
BTHR202
BVAL236
BSER240
BACP403
BHOH501
BHOH512
BHOH513
BHOH514
BHOH555
BHOH559

site_idAC9
Number of Residues5
Detailsbinding site for residue SO4 B 402
ChainResidue
BASN28
BARG180
BLYS224
BLYS325
BHOH535

site_idAD1
Number of Residues21
Detailsbinding site for residue ACP B 403
ChainResidue
BGLN187
BASN294
BPHE295
BASN297
BGLY330
BPRO331
BDGP401
BMG404
BHOH509
BHOH530
BHOH549
BHOH608
BGLY13
BSER14
BGLY16
BLYS17
BGLY18
BGLY42
BHIS43
BTHR44
BALA186

site_idAD2
Number of Residues5
Detailsbinding site for residue MG B 404
ChainResidue
BSER14
BTHR263
BARG269
BACP403
BHOH509

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_04166, ECO:0000305|PubMed:33926954
ChainResidueDetails
ASER14
BSER14

site_idSWS_FT_FI2
Number of Residues36
DetailsBINDING: BINDING => ECO:0000269|PubMed:33926955, ECO:0007744|PDB:6FM1
ChainResidueDetails
ASER14
ASER127
ATHR128
AARG142
AGLN187
ATHR202
ATHR263
AASN294
AASN297
AGLY330
BSER14
ATHR15
BTHR15
BGLY16
BLYS17
BGLY18
BASN40
BGLY42
BHIS43
BTHR44
BSER127
BTHR128
AGLY16
BARG142
BGLN187
BTHR202
BTHR263
BASN294
BASN297
BGLY330
ALYS17
AGLY18
AASN40
AGLY42
AHIS43
ATHR44

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:33926955, ECO:0007744|PDB:6TNH
ChainResidueDetails
AVAL264
AARG269
BVAL264
BARG269

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PDB entries from 2024-07-10

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