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4PDZ

Crystal Structure of Calcium-loaded S100B bound to SBi4172

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_idAC1
Number of Residues6
Detailsbinding site for residue CA A 101
ChainResidue
ASER18
AGLU21
AASP23
ALYS26
AGLU31
AHOH217

site_idAC2
Number of Residues6
Detailsbinding site for residue CA A 102
ChainResidue
AGLU67
AGLU72
AHOH237
AASP61
AASP63
AASP65

site_idAC3
Number of Residues6
Detailsbinding site for residue CA B 102
ChainResidue
BSER18
BGLU21
BASP23
BLYS26
BGLU31
BHOH209

site_idAC4
Number of Residues6
Detailsbinding site for residue CA B 103
ChainResidue
BASP61
BASP63
BASP65
BGLU67
BGLU72
BHOH220

site_idAC5
Number of Residues13
Detailsbinding site for Di-peptide CTI B 101 and CYS B 84
ChainResidue
AVAL7
AVAL8
AILE11
BPHE43
BILE80
BTHR81
BTHR82
BALA83
BHIS85
BGLU86
BPHE87
BPHE88
BHOH230

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
AGLU21
AASP23
AHIS25
AHIS85
AHIS90
BHIS15
BSER18
BGLU21
BASP23
BHIS25
BHIS85
BHIS90
AHIS15
ASER18

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448
ChainResidueDetails
AASP65
AGLU67
AGLU72
BASP61
BASP63
BASP65
BGLU67
BGLU72
AASP61
AASP63

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N-acetylserine => ECO:0000269|PubMed:4026304
ChainResidueDetails
ASER1
BSER1

219140

PDB entries from 2024-05-01

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