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1R6X

The Crystal Structure of a Truncated Form of Yeast ATP Sulfurylase, Lacking the C-Terminal APS Kinase-like Domain, in complex with Sulfate

Functional Information from GO Data
ChainGOidnamespacecontents
A0000103biological_processsulfate assimilation
A0004781molecular_functionsulfate adenylyltransferase (ATP) activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 2002
ChainResidue
AGLN195
AARG197
AALA293
AHOH4071
AHOH4111
AHOH4205
AHOH4393

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 2004
ChainResidue
AASP168
AARG173
AHOH4184
AHOH4265
AHOH4407
AHIS166
ATYR167

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 2005
ChainResidue
AARG205
AARG213
AHOH4364

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO A 3000
ChainResidue
AASP168
AHIS235
AHIS236
AHOH4265
AHOH4355

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 Residues3
DetailsAnnotated By Reference To The Literature 1j70
ChainResidueDetails
AHIS204
AHIS201
AARG197

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1j70
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 2024-11-06

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