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2IEW

Crystal structure of Inositol Phosphate Multikinase Ipk2 from S. cerevisiae

Functional Information from GO Data
ChainGOidnamespacecontents
A0000122biological_processnegative regulation of transcription by RNA polymerase II
A0000821biological_processregulation of arginine metabolic process
A0000823molecular_functioninositol-1,4,5-trisphosphate 6-kinase activity
A0000824molecular_functioninositol tetrakisphosphate 3-kinase activity
A0000825molecular_functioninositol tetrakisphosphate 6-kinase activity
A0000827molecular_functioninositol-1,3,4,5,6-pentakisphosphate kinase activity
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0006525biological_processarginine metabolic process
A0008440molecular_functioninositol-1,4,5-trisphosphate 3-kinase activity
A0016236biological_processmacroautophagy
A0016301molecular_functionkinase activity
A0016303molecular_function1-phosphatidylinositol-3-kinase activity
A0030674molecular_functionprotein-macromolecule adaptor activity
A0032958biological_processinositol phosphate biosynthetic process
A0036092biological_processphosphatidylinositol-3-phosphate biosynthetic process
A0045944biological_processpositive regulation of transcription by RNA polymerase II
A0046854biological_processphosphatidylinositol phosphate biosynthetic process
A0046872molecular_functionmetal ion binding
A0046934molecular_function1-phosphatidylinositol-4,5-bisphosphate 3-kinase activity
A0050821biological_processprotein stabilization
A0090575cellular_componentRNA polymerase II transcription regulator complex
B0000122biological_processnegative regulation of transcription by RNA polymerase II
B0000821biological_processregulation of arginine metabolic process
B0000823molecular_functioninositol-1,4,5-trisphosphate 6-kinase activity
B0000824molecular_functioninositol tetrakisphosphate 3-kinase activity
B0000825molecular_functioninositol tetrakisphosphate 6-kinase activity
B0000827molecular_functioninositol-1,3,4,5,6-pentakisphosphate kinase activity
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0006525biological_processarginine metabolic process
B0008440molecular_functioninositol-1,4,5-trisphosphate 3-kinase activity
B0016236biological_processmacroautophagy
B0016301molecular_functionkinase activity
B0016303molecular_function1-phosphatidylinositol-3-kinase activity
B0030674molecular_functionprotein-macromolecule adaptor activity
B0032958biological_processinositol phosphate biosynthetic process
B0036092biological_processphosphatidylinositol-3-phosphate biosynthetic process
B0045944biological_processpositive regulation of transcription by RNA polymerase II
B0046854biological_processphosphatidylinositol phosphate biosynthetic process
B0046872molecular_functionmetal ion binding
B0046934molecular_function1-phosphatidylinositol-4,5-bisphosphate 3-kinase activity
B0050821biological_processprotein stabilization
B0090575cellular_componentRNA polymerase II transcription regulator complex
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 501
ChainResidue
AGLU271
AASN274
AGLY334
AHOH524
AHOH537
AHOH681
AHOH706

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:17050532, ECO:0007744|PDB:2IF8
ChainResidueDetails
AASP131
AASP325
BLYS31
BGLU118
BASP131
BASP325
ALYS31
AGLU118

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
APRO127
BPRO127

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:17050532, ECO:0007744|PDB:2IEW, ECO:0007744|PDB:2IF8
ChainResidueDetails
BGLU271
BGLY334
AGLU271
AGLY334

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:17050532, ECO:0007744|PDB:2IEW
ChainResidueDetails
AASN274
BASN274

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N-acetylmethionine => ECO:0007744|PubMed:22814378
ChainResidueDetails
AMET1
BMET1

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19779198
ChainResidueDetails
ASER97
BSER97

221051

PDB entries from 2024-06-12

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