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1G8F

ATP SULFURYLASE FROM S. CEREVISIAE

Functional Information from GO Data
ChainGOidnamespacecontents
A0000096biological_processsulfur amino acid metabolic process
A0000103biological_processsulfate assimilation
A0004781molecular_functionsulfate adenylyltransferase (ATP) activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0006790biological_processsulfur compound metabolic process
A0010134biological_processsulfate assimilation via adenylyl sulfate reduction
A0016779molecular_functionnucleotidyltransferase activity
A0019379biological_processsulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin)
A0070814biological_processhydrogen sulfide biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CD A 512
ChainResidue
AASP168
AHIS235
AHIS236
ASO4525
AACY535

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CD A 513
ChainResidue
AHOH1094
AHOH1102
APRO39
ACYS43
AHOH895
AHOH1021

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CD A 514
ChainResidue
ALEU18
AGLU22
AHIS319
AACY526
AHOH1033

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CD A 515
ChainResidue
AGLU182
AGLU182
AACY533
AACY533

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CD A 516
ChainResidue
AASP189
AHIS494
AACY527
AACY534

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CA A 517
ChainResidue
AASP151

site_idAC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE NA A 518
ChainResidue
AGLU409

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CA A 519
ChainResidue
AASP303
AACY536

site_idAC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CA A 520
ChainResidue
AASP489
AASP489

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 521
ChainResidue
AGLU46
APRO164
AHIS166
AHOH604
AHOH1101

site_idBC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE NA A 522
ChainResidue
AASP309

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 523
ChainResidue
AGLN195
AARG197
AALA293
AHOH779
AHOH809
AHOH990

site_idBC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 525
ChainResidue
AHIS166
AASP168
AARG173
AHIS235
ASER417
ACD512
AACY535
AHOH553
AHOH733

site_idBC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE TRS A 524
ChainResidue
APRO2
AASP189
AGLY282
AHOH617
AHOH874

site_idBC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE ACY A 526
ChainResidue
AALA17
ALEU18
ALYS20
AASN21
AGLU22
AHIS319
ACD514
AHOH812

site_idBC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACY A 527
ChainResidue
AGLN187
AASP189
ASER493
AHIS494
ACD516
AACY534
AHOH692

site_idBC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACY A 528
ChainResidue
AASN216
AGLU486
AGLU490
APRO491
AHIS494
ALYS498

site_idBC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACY A 529
ChainResidue
ALYS174
AGLN178
ALEU181
AGLU182
AGLU182
ASER185

site_idCC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACY A 530
ChainResidue
AGLU130
AARG134

site_idCC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACY A 531
ChainResidue
APRO55
ALEU56
ATHR57
AGLY58
AASP64
AHOH719

site_idCC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACY A 532
ChainResidue
AASP71
AASP71

site_idCC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE ACY A 533
ChainResidue
ACD515
ACD515
AHOH561
AGLY171
ALYS174
AGLU182
AGLU182
AARG186
APHE255

site_idCC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACY A 534
ChainResidue
AASP189
AHIS494
ACD516
AACY527
AHOH671

site_idCC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACY A 535
ChainResidue
AASP168
AHIS235
AHIS236
ASER417
ACD512
ASO4525

site_idCC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACY A 536
ChainResidue
ALYS297
AGLY301
AVAL302
AASP303
ACA519

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_03106, ECO:0000305|PubMed:11157739
ChainResidueDetails
ATHR196
AARG197
AASN198

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03106, ECO:0000269|PubMed:11157739
ChainResidueDetails
AGLN195
AARG197
AGLY289
AALA293
AVAL331

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_03106, ECO:0000305|PubMed:11157739
ChainResidueDetails
AHIS201
AHIS204

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Induces change in substrate recognition on ATP binding => ECO:0000255|HAMAP-Rule:MF_03106, ECO:0000305|PubMed:11157739
ChainResidueDetails
APHE328

Catalytic Information from CSA
site_idCSA1
Number of Residues1
Detailsa catalytic site defined by CSA, PubMed 11157739
ChainResidueDetails
AARG290

site_idMCSA1
Number of Residues5
DetailsM-CSA 287
ChainResidueDetails
ATHR196electrostatic stabiliser, hydrogen bond donor, steric role
AARG197electrostatic stabiliser, hydrogen bond donor, steric role
AHIS201hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AHIS204electrostatic stabiliser
AARG290electrostatic stabiliser

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PDB entries from 2024-07-24

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