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1OMD

STRUCTURE OF ONCOMODULIN REFINED AT 1.85 ANGSTROMS RESOLUTION. AN EXAMPLE OF EXTENSIVE MOLECULAR AGGREGATION VIA CA2+

Functional Information from GO Data
ChainGOidnamespacecontents
A0005509molecular_functioncalcium ion binding
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0009611biological_processresponse to wounding
A0031982cellular_componentvesicle
A0032420cellular_componentstereocilium
A0032437cellular_componentcuticular plate
A0032991cellular_componentprotein-containing complex
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0044877molecular_functionprotein-containing complex binding
A0046872molecular_functionmetal ion binding
A0090102biological_processcochlea development
A0099512cellular_componentsupramolecular fiber
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 109
ChainResidue
AASP90
AASP92
AASP94
ALYS96
AGLU101
AHOH111

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 110
ChainResidue
AASP51
AASP53
ASER55
ATYR57
AGLU62
AHOH112

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 135
ChainResidue
AGLN54
AGLN71
AASP73
AGLU79
AHOH169
AHOH172

site_idCD
Number of Residues12
DetailsCALCIUM BINDING SITE 1
ChainResidue
AASP51
AGLY60
AASP61
AGLU62
AASN52
AASP53
AGLN54
ASER55
AGLY56
ATYR57
ALEU58
AASP59

site_idEF
Number of Residues12
DetailsCALCIUM BINDING SITE 2
ChainResidue
AASP90
AASN91
AASP92
AGLY93
AASP94
AGLY95
ALYS96
AILE97
AGLY98
AALA99
AASP100
AGLU101

Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DNDQSGYLDgdEL
ChainResidueDetails
AASP51-LEU63
AASP90-PHE102

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448
ChainResidueDetails
AASN52
APHE102
AGLN54
AGLY56
ALEU58
ALEU63
AASN91
AGLY93
AGLY95
AILE97

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N-acetylserine => ECO:0000269|PubMed:6617664
ChainResidueDetails
AILE2

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PDB entries from 2024-07-24

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