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2M49

Structural Insights into Human S100B and Basic Fibroblast Growth Factor (FGF2) Interaction

Functional Information from GO Data
ChainGOidnamespacecontents
A0008083molecular_functiongrowth factor activity
B0001726cellular_componentruffle
B0005509molecular_functioncalcium ion binding
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0007155biological_processcell adhesion
B0007409biological_processaxonogenesis
B0007417biological_processcentral nervous system development
B0007611biological_processlearning or memory
B0007613biological_processmemory
B0008270molecular_functionzinc ion binding
B0008284biological_processpositive regulation of cell population proliferation
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0043025cellular_componentneuronal cell body
B0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
B0043231cellular_componentintracellular membrane-bounded organelle
B0044548molecular_functionS100 protein binding
B0045666biological_processpositive regulation of neuron differentiation
B0046872molecular_functionmetal ion binding
B0048156molecular_functiontau protein binding
B0048168biological_processregulation of neuronal synaptic plasticity
B0048306molecular_functioncalcium-dependent protein binding
B0048471cellular_componentperinuclear region of cytoplasm
B0050786molecular_functionRAGE receptor binding
B0097490biological_processsympathetic neuron projection extension
B1990138biological_processneuron projection extension
B1990845biological_processadaptive thermogenesis
C0008083molecular_functiongrowth factor activity
D0001726cellular_componentruffle
D0005509molecular_functioncalcium ion binding
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0005615cellular_componentextracellular space
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0007155biological_processcell adhesion
D0007409biological_processaxonogenesis
D0007417biological_processcentral nervous system development
D0007611biological_processlearning or memory
D0007613biological_processmemory
D0008270molecular_functionzinc ion binding
D0008284biological_processpositive regulation of cell population proliferation
D0042802molecular_functionidentical protein binding
D0042803molecular_functionprotein homodimerization activity
D0043025cellular_componentneuronal cell body
D0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
D0043231cellular_componentintracellular membrane-bounded organelle
D0044548molecular_functionS100 protein binding
D0045666biological_processpositive regulation of neuron differentiation
D0046872molecular_functionmetal ion binding
D0048156molecular_functiontau protein binding
D0048168biological_processregulation of neuronal synaptic plasticity
D0048306molecular_functioncalcium-dependent protein binding
D0048471cellular_componentperinuclear region of cytoplasm
D0050786molecular_functionRAGE receptor binding
D0097490biological_processsympathetic neuron projection extension
D1990138biological_processneuron projection extension
D1990845biological_processadaptive thermogenesis
Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DNDGDGECDfqEF
ChainResidueDetails
BASP61-PHE73

site_idPS00247
Number of Residues24
DetailsHBGF_FGF HBGF/FGF family signature. GrLlAsksvtd.ECfFfErlesnnY
ChainResidueDetails
AGLY80-TYR103

site_idPS00303
Number of Residues22
DetailsS100_CABP S-100/ICaBP type calcium binding protein signature. VMetLDndgDgecDFqEFmaFV
ChainResidueDetails
BVAL56-VAL77

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:20950652, ECO:0007744|PDB:3CZT
ChainResidueDetails
BHIS15
BHIS25
BHIS85
BHIS90
DHIS106
DHIS116
DHIS176
DHIS181

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:20950652, ECO:0007744|PDB:3CZT, ECO:0007744|PDB:3D0Y, ECO:0007744|PDB:3D10
ChainResidueDetails
BSER18
DGLU122
BGLU21
BASP23
BLYS26
BGLU31
DSER109
DGLU112
DASP114
DLYS117

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:20950652, ECO:0007744|PDB:3CZT, ECO:0007744|PDB:3D0Y, ECO:0007744|PDB:3D10
ChainResidueDetails
BASP61
BASP65
BGLU67
BGLU72
DASP152
DASP156
DGLU158
DGLU163

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:20950652, ECO:0007744|PDB:2H61, ECO:0007744|PDB:3CZT, ECO:0007744|PDB:3D0Y, ECO:0007744|PDB:3D10
ChainResidueDetails
BASP63
DASP154
CLYS86

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N-acetylserine; alternate => ECO:0000250|UniProtKB:P02638
ChainResidueDetails
BSER1
DSER92

221716

PDB entries from 2024-06-26

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