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6RM2

Deoxyguanylosuccinate synthase (DgsS) structure with ATP, IMP, Magnesium

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 Residues20
Detailsbinding site for residue ATP A 401
ChainResidue
ASER14
AARG269
AASN294
APHE295
AASN297
AGLY330
APRO331
AMG402
AHOH509
AHOH528
AHOH531
ATHR15
AHOH565
AGLY16
ALYS17
AGLY18
ALEU19
AGLY42
AHIS43
ATHR44

site_idAC2
Number of Residues4
Detailsbinding site for residue MG A 402
ChainResidue
ASER14
AALA41
AGLY42
AATP401

site_idAC3
Number of Residues15
Detailsbinding site for residue IMP A 403
ChainResidue
ASER14
AASN40
AALA41
AGLY126
ASER127
ATHR128
AGLN187
ALEU191
ACYS201
ATHR202
AVAL236
AHOH531
AHOH549
AHOH551
BARG142

site_idAC4
Number of Residues4
Detailsbinding site for residue SO4 A 404
ChainResidue
AASN28
AARG180
ALYS224
AHOH522

site_idAC5
Number of Residues16
Detailsbinding site for residue ATP B 401
ChainResidue
BSER14
BTHR15
BGLY16
BLYS17
BGLY18
BGLY42
BHIS43
BTHR44
BTHR263
BARG269
BASN294
BPHE295
BASN297
BGLY330
BPRO331
BMG402

site_idAC6
Number of Residues4
Detailsbinding site for residue MG B 402
ChainResidue
BSER14
BGLY42
BTHR263
BATP401

site_idAC7
Number of Residues18
Detailsbinding site for residue IMP B 403
ChainResidue
AARG142
BPHE12
BSER14
BASN40
BALA41
BILE125
BSER127
BTHR128
BGLN187
BLEU191
BCYS201
BTHR202
BVAL236
BSER240
BHOH505
BHOH514
BHOH546
BHOH553

site_idAC8
Number of Residues7
Detailsbinding site for residue SO4 B 404
ChainResidue
BASN334
BASN334
BVAL336
BGLU337
BGLU337
BHOH513
BHOH513

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 2024-07-17

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