Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2F49

Crystal structure of Fus3 in complex with a Ste5 peptide

Functional Information from GO Data
ChainGOidnamespacecontents
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
A0004705molecular_functionJUN kinase activity
A0004707molecular_functionMAP kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0006468biological_processprotein phosphorylation
A0007254biological_processJNK cascade
A0010494cellular_componentcytoplasmic stress granule
A0010526biological_processretrotransposon silencing
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
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
B0004705molecular_functionJUN kinase activity
B0004707molecular_functionMAP kinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0006468biological_processprotein phosphorylation
B0007254biological_processJNK cascade
B0010494cellular_componentcytoplasmic stress granule
B0010526biological_processretrotransposon silencing
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 Residues4
DetailsBINDING SITE FOR RESIDUE MG A 601
ChainResidue
ATYR24
AGLY25
AGLU45
ALYS49

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG B 602
ChainResidue
BTYR24
BGLY25
BGLU45
BLYS49

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SCN A 501
ChainResidue
AILE44
ALYS42

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SCN B 503
ChainResidue
ALYS49
APRO50
ALEU51
APHE52
BLYS49
BPRO50
BLEU51
BPHE52

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SCN B 504
ChainResidue
AALA337
BARG189
BVAL193
BLYS199

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SCN A 505
ChainResidue
AARG189
AVAL193
AMET194
ALYS199
BGLU336
BALA337

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SCN A 506
ChainResidue
ATHR185
AARG186
ATRP187
BTHR339

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SCN B 507
ChainResidue
ALYS341
BTHR185
BARG186
BTRP187
BGLY225
BHOH624
BHOH666
BHOH702

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 Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP137
BASP137

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU19
ALYS42
BLEU19
BLYS42

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:1628831
ChainResidueDetails
AVAL180
BVAL180

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:1628831
ChainResidueDetails
APHE182
BPHE182

site_idSWS_FT_FI5
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
ChainResidueDetails
ALYS345
BLYS345

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

227111

PDB entries from 2024-11-06

PDB statisticsPDBj update infoContact PDBjnumon