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2FA2

Crystal structure of Fus3 without a peptide from Ste5

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000749biological_processresponse to pheromone triggering conjugation with cellular fusion
A0000750biological_processpheromone-dependent signal transduction involved in conjugation with cellular fusion
A0001403biological_processinvasive growth in response to glucose limitation
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0004707molecular_functionMAP kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0006468biological_processprotein phosphorylation
A0010494cellular_componentcytoplasmic stress granule
A0010526biological_processtransposable element silencing
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0035556biological_processintracellular signal transduction
A0042597cellular_componentperiplasmic space
A0042802molecular_functionidentical protein binding
A0043332cellular_componentmating projection tip
A0043409biological_processnegative regulation of MAPK cascade
A0046827biological_processpositive regulation of protein export from nucleus
A0051301biological_processcell division
A0071507biological_processpheromone response MAPK cascade
A0106310molecular_functionprotein serine kinase activity
B0000166molecular_functionnucleotide binding
B0000749biological_processresponse to pheromone triggering conjugation with cellular fusion
B0000750biological_processpheromone-dependent signal transduction involved in conjugation with cellular fusion
B0001403biological_processinvasive growth in response to glucose limitation
B0004672molecular_functionprotein kinase activity
B0004674molecular_functionprotein serine/threonine kinase activity
B0004707molecular_functionMAP kinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0006468biological_processprotein phosphorylation
B0010494cellular_componentcytoplasmic stress granule
B0010526biological_processtransposable element silencing
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0035556biological_processintracellular signal transduction
B0042597cellular_componentperiplasmic space
B0042802molecular_functionidentical protein binding
B0043332cellular_componentmating projection tip
B0043409biological_processnegative regulation of MAPK cascade
B0046827biological_processpositive regulation of protein export from nucleus
B0051301biological_processcell division
B0071507biological_processpheromone response MAPK cascade
B0106310molecular_functionprotein serine kinase activity
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SCN A 501
ChainResidue
ALYS42
AILE44

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SCN B 502
ChainResidue
ALEU51
BLYS49
BPRO50
BLEU51
BPHE52

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SCN B 503
ChainResidue
BARG189
BVAL193
BMET194
BLYS199
AGLU336
AALA337

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SCN A 504
ChainResidue
AARG189
AVAL193
AMET194
ALYS199
BALA337

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SCN A 505
ChainResidue
ATHR185
BTHR339

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SCN B 506
ChainResidue
ATHR339
ALYS341
BTHR185
BARG186

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues25
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGAYGVVCsAthkptgeiv.........AIKK
ChainResidueDetails
ALEU19-LYS43

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ViHrDLKpsNLLI
ChainResidueDetails
AVAL133-ILE145

site_idPS01351
Number of Residues103
DetailsMAPK MAP kinase signature. FdkplfalrtlREikilkhfkheniitifniqrpdsfenfnevyiiqelmqtdlhrvistqmlsddhiqyfiyqtlravkvlhgsnvih..........RDlKpsnllinsnC
ChainResidueDetails
APHE47-CYS149

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsMotif: {"description":"TXY"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues18
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"1628831","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"1628831","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"22106047","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ASER141
AASP137

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BSER141
BASP137

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ALYS139
AASP137

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BLYS139
BASP137

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ATHR185
ALYS139
AASP137

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BTHR185
BLYS139
BASP137

site_idCSA7
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASN142
ALYS139
AASP137

site_idCSA8
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASN142
BLYS139
BASP137

239803

PDB entries from 2025-08-06

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