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3D0Y

Crystal Structure of S100B in the Calcium and Zinc Loaded State at pH 6.5

Functional Information from GO Data
ChainGOidnamespacecontents
A0001726cellular_componentruffle
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0007155biological_processcell adhesion
A0007409biological_processaxonogenesis
A0007417biological_processcentral nervous system development
A0007611biological_processlearning or memory
A0007613biological_processmemory
A0008270molecular_functionzinc ion binding
A0008284biological_processpositive regulation of cell population proliferation
A0016529cellular_componentsarcoplasmic reticulum
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0043025cellular_componentneuronal cell body
A0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
A0043167molecular_functionion binding
A0043231cellular_componentintracellular membrane-bounded organelle
A0044548molecular_functionS100 protein binding
A0045666biological_processpositive regulation of neuron differentiation
A0046872molecular_functionmetal ion binding
A0048156molecular_functiontau protein binding
A0048168biological_processregulation of neuronal synaptic plasticity
A0048306molecular_functioncalcium-dependent protein binding
A0048471cellular_componentperinuclear region of cytoplasm
A0050786molecular_functionRAGE receptor binding
A0097490biological_processsympathetic neuron projection extension
A1990138biological_processneuron projection extension
A1990845biological_processadaptive thermogenesis
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
B0016529cellular_componentsarcoplasmic reticulum
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0043025cellular_componentneuronal cell body
B0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
B0043167molecular_functionion binding
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
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 92
ChainResidue
AASP61
AASP63
AASP65
AGLU67
AGLU72

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 93
ChainResidue
AGLU31
ASER18
AGLU21
AASP23
ALYS26

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 92
ChainResidue
BSER18
BGLU21
BASP23
BLYS26
BGLU31

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 93
ChainResidue
BASP61
BASP63
BASP65
BGLU67
BGLU72

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 94
ChainResidue
AHIS15
AHIS25
BHIS85
BGLU89

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 95
ChainResidue
AHIS85
AGLU89
BHIS15
BHIS25

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PG4 B 94
ChainResidue
BHIS42
BPHE43
BGLU45
BALA83
BCYS84

Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DNDGDGECDfqEF
ChainResidueDetails
BASP61-PHE73
AASP61-PHE73

site_idPS00303
Number of Residues22
DetailsS100_CABP S-100/ICaBP type calcium binding protein signature. VMetLDndgDgecDFqEFmaFV
ChainResidueDetails
BVAL56-VAL77
AVAL56-VAL77

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:20950652, ECO:0007744|PDB:3CZT
ChainResidueDetails
BHIS15
BHIS25
BHIS85
BHIS90

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:20950652, ECO:0007744|PDB:3CZT, ECO:0007744|PDB:3D0Y, ECO:0007744|PDB:3D10
ChainResidueDetails
BSER18
BGLU21
BASP23
BLYS26
BGLU31

site_idSWS_FT_FI3
Number of Residues4
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

site_idSWS_FT_FI4
Number of Residues1
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

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N-acetylserine; alternate => ECO:0000250|UniProtKB:P02638
ChainResidueDetails
BSER1

218853

PDB entries from 2024-04-24

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