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1CFP

S100B (S100BETA) NMR DATA WAS COLLECTED FROM A SAMPLE OF CALCIUM FREE PROTEIN AT PH 6.3 AND A TEMPERATURE OF 311 K AND 1.7-6.9 MM CONCENTRATION, 25 STRUCTURES

Functional Information from GO Data
ChainGOidnamespacecontents
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0006417biological_processregulation of translation
A0007155biological_processcell adhesion
A0007409biological_processaxonogenesis
A0007611biological_processlearning or memory
A0008270molecular_functionzinc ion binding
A0008284biological_processpositive regulation of cell population proliferation
A0016310biological_processphosphorylation
A0019210molecular_functionkinase inhibitor activity
A0042803molecular_functionprotein homodimerization activity
A0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
A0044548molecular_functionS100 protein binding
A0045917biological_processpositive regulation of complement activation
A0046872molecular_functionmetal ion binding
A0048143biological_processastrocyte activation
A0048156molecular_functiontau protein binding
A0048306molecular_functioncalcium-dependent protein binding
A0050786molecular_functionRAGE receptor binding
A0071638biological_processnegative regulation of monocyte chemotactic protein-1 production
A0097490biological_processsympathetic neuron projection extension
A1990845biological_processadaptive thermogenesis
B0005509molecular_functioncalcium ion binding
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0006417biological_processregulation of translation
B0007155biological_processcell adhesion
B0007409biological_processaxonogenesis
B0007611biological_processlearning or memory
B0008270molecular_functionzinc ion binding
B0008284biological_processpositive regulation of cell population proliferation
B0016310biological_processphosphorylation
B0019210molecular_functionkinase inhibitor activity
B0042803molecular_functionprotein homodimerization activity
B0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
B0044548molecular_functionS100 protein binding
B0045917biological_processpositive regulation of complement activation
B0046872molecular_functionmetal ion binding
B0048143biological_processastrocyte activation
B0048156molecular_functiontau protein binding
B0048306molecular_functioncalcium-dependent protein binding
B0050786molecular_functionRAGE receptor binding
B0071638biological_processnegative regulation of monocyte chemotactic protein-1 production
B0097490biological_processsympathetic neuron projection extension
B1990845biological_processadaptive thermogenesis
Functional Information from PDB Data
site_idLOA
Number of Residues14
DetailsLOW AFFINITY HELIX-LOOP-HELIX CALCIUM BINDING LOOP.
ChainResidue
ASER18
ALEU27
ALYS28
ALYS29
ASER30
AGLU31
AGLY19
AARG20
AGLU21
AGLY22
AASP23
ALYS24
AHIS25
ALYS26

site_idLOB
Number of Residues12
DetailsHIGH AFFINITY HELIX-LOOP-HELIX CALCIUM BINDING LOOP.
ChainResidue
AASP61
ASER62
AASP63
AGLY64
AASP65
AGLY66
AGLU67
ACYS68
AASP69
APHE70
AGLN71
AGLU72

site_idLOC
Number of Residues14
DetailsLOW AFFINITY HELIX-LOOP-HELIX CALCIUM BINDING LOOP.
ChainResidue
BSER18
BGLY19
BARG20
BGLU21
BGLY22
BASP23
BLYS24
BHIS25
BLYS26
BLEU27
BLYS28
BLYS29
BSER30
BGLU31

site_idLOD
Number of Residues12
DetailsHIGH AFFINITY HELIX-LOOP-HELIX CALCIUM BINDING LOOP.
ChainResidue
BASP61
BSER62
BASP63
BGLY64
BASP65
BGLY66
BGLU67
BCYS68
BASP69
BPHE70
BGLN71
BGLU72

Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DSDGDGECDfqEF
ChainResidueDetails
AASP61-PHE73

site_idPS00303
Number of Residues22
DetailsS100_CABP S-100/ICaBP type calcium binding protein signature. VMetLDsdgDgecDFqEFmaFV
ChainResidueDetails
AVAL56-VAL77

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P04271
ChainResidueDetails
AGLN16
BGLY22
BLYS24
BLYS26
BGLU86
BGLU91
AGLY19
AGLY22
ALYS24
ALYS26
AGLU86
AGLU91
BGLN16
BGLY19

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448
ChainResidueDetails
ASER62
BPHE73
AGLY64
AGLY66
ACYS68
APHE73
BSER62
BGLY64
BGLY66
BCYS68

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N-acetylserine => ECO:0000269|PubMed:4026304
ChainResidueDetails
AGLU2
BGLU2

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PDB entries from 2024-11-13

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