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2JPT

Structural changes induced in apo-s100a1 protein by the disulphide formation between its CYS85 residue and b-mercaptoethanol

Functional Information from GO Data
ChainGOidnamespacecontents
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005794cellular_componentGolgi apparatus
A0005829cellular_componentcytosol
A0008016biological_processregulation of heart contraction
A0016529cellular_componentsarcoplasmic reticulum
A0042311biological_processvasodilation
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0044548molecular_functionS100 protein binding
A0046872molecular_functionmetal ion binding
A0048306molecular_functioncalcium-dependent protein binding
A0051117molecular_functionATPase binding
A1903672biological_processpositive regulation of sprouting angiogenesis
B0005509molecular_functioncalcium ion binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005794cellular_componentGolgi apparatus
B0005829cellular_componentcytosol
B0008016biological_processregulation of heart contraction
B0016529cellular_componentsarcoplasmic reticulum
B0042311biological_processvasodilation
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0044548molecular_functionS100 protein binding
B0046872molecular_functionmetal ion binding
B0048306molecular_functioncalcium-dependent protein binding
B0051117molecular_functionATPase binding
B1903672biological_processpositive regulation of sprouting angiogenesis
Functional Information from PDB Data
site_idAC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE BME A 94
ChainResidue
ACYS85

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE BME B 94
ChainResidue
BCYS85

Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DEDGDGEVDfqEY
ChainResidueDetails
AASP62-TYR74

site_idPS00303
Number of Residues22
DetailsS100_CABP S-100/ICaBP type calcium binding protein signature. VMkeLDedgDgevDFqEYvvLV
ChainResidueDetails
AVAL57-VAL78

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P35467
ChainResidueDetails
ALYS27
AGLU32
BLYS27
BGLU32

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448
ChainResidueDetails
AASP62
BGLU73
AASP64
AASP66
AGLU68
AGLU73
BASP62
BASP64
BASP66
BGLU68

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Blocked amino end (Gly) => ECO:0000269|PubMed:7250124
ChainResidueDetails
AGLY1
BGLY1

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:P23297
ChainResidueDetails
ACYS85
BCYS85

237735

PDB entries from 2025-06-18

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