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6FM1

Deoxyguanylosuccinate synthase (DgsS) quaternary structure with ATPanddGMP at 2.3 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 Residues22
Detailsbinding site for residue ATP A 401
ChainResidue
AGLY13
ATHR44
AALA186
AGLN187
AARG269
AASN294
APHE295
AASN297
AGLY330
APRO331
ADGP402
ASER14
AMG403
AHOH503
AHOH508
ATHR15
AGLY16
ALYS17
AGLY18
AALA41
AGLY42
AHIS43

site_idAC2
Number of Residues22
Detailsbinding site for residue DGP A 402
ChainResidue
APHE12
ASER14
AASN40
AALA41
AILE125
AGLY126
ASER127
ATHR128
AGLN187
ALEU191
ACYS201
ATHR202
AVAL236
ASER240
AATP401
AHOH527
AHOH535
AHOH550
AHOH551
AHOH605
AHOH623
BARG142

site_idAC3
Number of Residues4
Detailsbinding site for residue MG A 403
ChainResidue
ASER14
AGLY42
ATHR263
AATP401

site_idAC4
Number of Residues4
Detailsbinding site for residue CL A 404
ChainResidue
AASN28
AARG180
ALYS224
ATYR326

site_idAC5
Number of Residues4
Detailsbinding site for residue GOL A 405
ChainResidue
ATYR200
ATHR239
AGLY241
AGLY242

site_idAC6
Number of Residues7
Detailsbinding site for residue GOL A 406
ChainResidue
AILE87
ALYS91
ALEU94
AILE100
ATYR164
AHOH554
AHOH603

site_idAC7
Number of Residues25
Detailsbinding site for residue ATP B 401
ChainResidue
BGLY13
BSER14
BTHR15
BGLY16
BLYS17
BGLY18
BALA41
BGLY42
BHIS43
BTHR44
BGLN187
BASN294
BPHE295
BASN297
BGLY330
BPRO331
BDGP402
BMG403
BHOH505
BHOH528
BHOH541
BHOH653
BHOH671
BHOH683
BHOH686

site_idAC8
Number of Residues21
Detailsbinding site for residue DGP B 402
ChainResidue
BTHR202
BVAL236
BSER240
BATP401
BHOH513
BHOH531
BHOH542
BHOH577
BHOH586
BHOH604
AARG142
BPHE12
BSER14
BASN40
BALA41
BGLY126
BSER127
BTHR128
BGLN187
BLEU191
BCYS201

site_idAC9
Number of Residues4
Detailsbinding site for residue MG B 403
ChainResidue
BSER14
BGLY42
BARG269
BATP401

site_idAD1
Number of Residues4
Detailsbinding site for residue GOL B 404
ChainResidue
BGLU26
BASN47
BTRP53
BHOH601

site_idAD2
Number of Residues4
Detailsbinding site for residue GOL B 405
ChainResidue
BPHE329
BVAL342
BHOH558
BHOH731

site_idAD3
Number of Residues8
Detailsbinding site for residue GOL B 406
ChainResidue
AMET1
APRO220
BGLN287
BPRO288
BASP289
BTYR319
BASP321
BALA322

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
AGLY16
ALYS17
AGLY18
AASN40
AGLY42
AHIS43
ATHR44
ASER127
ATHR128
AARG142
AGLN187
ATHR202
ATHR263
AASN294
AASN297
AGLY330
BSER14
BTHR15
BGLY16
BLYS17
BGLY18
BASN40
BGLY42
BHIS43
BTHR44
BSER127
BTHR128
BARG142
BGLN187
BTHR202
BTHR263
BASN294
BASN297
BGLY330
ASER14
ATHR15

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

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PDB entries from 2024-04-17

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