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1QGX

X-RAY STRUCTURE OF YEAST HAL2P

Functional Information from GO Data
ChainGOidnamespacecontents
A0000103biological_processsulfate assimilation
A0005575cellular_componentcellular_component
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0006790biological_processsulfur compound metabolic process
A0008441molecular_function3'(2'),5'-bisphosphate nucleotidase activity
A0009086biological_processmethionine biosynthetic process
A0016078biological_processtRNA decay
A0016787molecular_functionhydrolase activity
A0016791molecular_functionphosphatase activity
A0042538biological_processhyperosmotic salinity response
A0046854biological_processphosphatidylinositol phosphate biosynthetic process
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 401
ChainResidue
AGLU72
AASP142
AILE144
APO4404
AHOH410

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 403
ChainResidue
AGLU72
APO4404
AHOH408
AHOH409
AHOH411

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PO4 A 404
ChainResidue
AGLU72
AASP142
AILE144
AASP145
AGLY146
ATHR147
AMG401
AMG403
AAMP405
ASO4406
AHOH414
AHOH760

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 406
ChainResidue
ASER43
APRO44
ALYS148
AHIS241
APO4404
AAMP405
AHOH409
AHOH414
AHOH758

site_idAC5
Number of Residues19
DetailsBINDING SITE FOR RESIDUE AMP A 405
ChainResidue
AASP142
AGLY240
AHIS241
AASP263
ASER264
ALYS267
AARG281
ATYR288
AGLU290
AASP294
APO4404
ASO4406
AHOH412
AHOH413
AHOH417
AHOH418
AHOH420
AHOH716
AHOH760

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE BME A 407
ChainResidue
ASER84
AMET313
ACYS349
AASP350
AGLN353
AHOH426

site_idS1
Number of Residues3
DetailsMAGNESIUM BINDING SITE
ChainResidue
AASP142
AILE144
AGLU72

site_idS3
Number of Residues1
DetailsMAGNESIUM BINDING SITE
ChainResidue
AGLU72

Functional Information from PROSITE/UniProt
site_idPS00629
Number of Residues14
DetailsIMP_1 Inositol monophosphatase family signature 1. WcLDPIDGTkgFlR
ChainResidueDetails
ATRP139-ARG152

site_idPS00630
Number of Residues15
DetailsIMP_2 Inositol monophosphatase family signature 2. WDhAAGnVIVheaGG
ChainResidueDetails
ATRP293-GLY307

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:12126627
ChainResidueDetails
AASP49
ATHR147

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:10656801, ECO:0000269|PubMed:12126627, ECO:0007744|PDB:1K9Y, ECO:0007744|PDB:1QGX
ChainResidueDetails
AGLU72
AILE144

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:12126627, ECO:0007744|PDB:1K9Y, ECO:0007744|PDB:1KA1
ChainResidueDetails
AASP142
AASP145
AASP294

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:12126627, ECO:0007744|PDB:1KA1
ChainResidueDetails
ATHR147

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:10656801, ECO:0000269|PubMed:12126627, ECO:0000269|Ref.10, ECO:0007744|PDB:1K9Y, ECO:0007744|PDB:1KA0, ECO:0007744|PDB:1QGX
ChainResidueDetails
AHIS241
ASER264
ALYS267
AARG281

Catalytic Information from CSA
site_idCSA1
Number of Residues3
Detailsa catalytic site defined by CSA, PubMed 12126627
ChainResidueDetails
AASP294
AASP49
ATHR147

site_idMCSA1
Number of Residues7
DetailsM-CSA 904
ChainResidueDetails
AASP49proton acceptor, proton donor
AGLU72metal ligand
AASP142metal ligand
AILE144metal ligand
AASP145metal ligand
ATHR147proton acceptor, proton donor, proton relay
AASP294metal ligand

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PDB entries from 2024-07-10

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