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2KBM

Ca-S100A1 interacting with TRTK12

Functional Information from GO Data
ChainGOidnamespacecontents
A0000122biological_processnegative regulation of transcription by RNA polymerase II
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0008016biological_processregulation of heart contraction
A0016529cellular_componentsarcoplasmic reticulum
A0030018cellular_componentZ disc
A0031430cellular_componentM band
A0031672cellular_componentA band
A0031674cellular_componentI band
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
B0000122biological_processnegative regulation of transcription by RNA polymerase II
B0005509molecular_functioncalcium ion binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0008016biological_processregulation of heart contraction
B0016529cellular_componentsarcoplasmic reticulum
B0030018cellular_componentZ disc
B0031430cellular_componentM band
B0031672cellular_componentA band
B0031674cellular_componentI band
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 Residues6
DetailsBINDING SITE FOR RESIDUE CA A 100
ChainResidue
AHIS18
ASER19
AGLU22
AGLY23
AASP24
ALEU28

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA B 101
ChainResidue
BSER19
BGLU22
BLYS27

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 102
ChainResidue
ALYS27
ALEU61
AASP62
AGLU63

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA B 103
ChainResidue
BASP62
BGLU63
BASN64

Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DENGDGEVDfqEF
ChainResidueDetails
AASP62-PHE74

site_idPS00303
Number of Residues22
DetailsS100_CABP S-100/ICaBP type calcium binding protein signature. IMkeLDengDgevDFqEFvvLV
ChainResidueDetails
AILE57-VAL78

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:16169012, ECO:0000269|PubMed:18650434, ECO:0000269|PubMed:19452629
ChainResidueDetails
ALYS27
AGLU32
BLYS27
BGLU32

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:16169012, ECO:0000269|PubMed:18650434, ECO:0000269|PubMed:19452629
ChainResidueDetails
AASP62
BGLU73
AASN64
AASP66
AGLU68
AGLU73
BASP62
BASN64
BASP66
BGLU68

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:P23297
ChainResidueDetails
ACYS85
BCYS85

219140

PDB entries from 2024-05-01

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