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

3HCM

Crystal structure of human S100B in complex with S45

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
ASER18
AGLU21
AASP23
ALYS26
AGLU31

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 93
ChainResidue
AGLU72
AHOH139
AASP61
AASP63
AASP65
AGLU67

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE S45 A 94
ChainResidue
ALEU44
ALEU60
APHE76
AMET79
AHOH143

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE ACT A 95
ChainResidue
AGLU45

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 92
ChainResidue
BSER18
BGLU21
BASP23
BLYS26
BGLU31
BHOH123

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 93
ChainResidue
BASP61
BASP63
BASP65
BGLU67
BGLU72
BHOH131

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE S45 B 94
ChainResidue
BLEU44
BGLU45
BVAL56
BPHE76
BMET79
BHOH127

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

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:20950652, ECO:0007744|PDB:3CZT
ChainResidueDetails
AHIS15
AHIS25
BHIS15
BHIS25
BHIS85
BHIS90
AHIS85
AHIS90

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
ASER18
AGLU21
AASP23
ALYS26
AGLU31
BSER18
BGLU21
BASP23
BLYS26
BGLU31

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
AGLU67
AGLU72
BASP61
BASP65
BGLU67
BGLU72
AASP61
AASP65

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
AASP63
BASP63

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N-acetylserine; alternate => ECO:0000250|UniProtKB:P02638
ChainResidueDetails
ASER1
BSER1

218500

PDB entries from 2024-04-17

PDB statisticsPDBj update infoContact PDBjnumon