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1RTP

REFINED X-RAY STRUCTURE OF RAT PARVALBUMIN, A MAMMALIAN ALPHA-LINEAGE PARVALBUMIN, AT 2.0 A RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
10005509molecular_functioncalcium ion binding
10005737cellular_componentcytoplasm
10010467biological_processgene expression
10030424cellular_componentaxon
10032420cellular_componentstereocilium
10032437cellular_componentcuticular plate
10032991cellular_componentprotein-containing complex
10042802molecular_functionidentical protein binding
10043025cellular_componentneuronal cell body
10043195cellular_componentterminal bouton
10044877molecular_functionprotein-containing complex binding
10046872molecular_functionmetal ion binding
10090102biological_processcochlea development
10098976biological_processexcitatory chemical synaptic transmission
10098977biological_processinhibitory chemical synaptic transmission
20005509molecular_functioncalcium ion binding
20005737cellular_componentcytoplasm
20010467biological_processgene expression
20030424cellular_componentaxon
20032420cellular_componentstereocilium
20032437cellular_componentcuticular plate
20032991cellular_componentprotein-containing complex
20042802molecular_functionidentical protein binding
20043025cellular_componentneuronal cell body
20043195cellular_componentterminal bouton
20044877molecular_functionprotein-containing complex binding
20046872molecular_functionmetal ion binding
20090102biological_processcochlea development
20098976biological_processexcitatory chemical synaptic transmission
20098977biological_processinhibitory chemical synaptic transmission
30005509molecular_functioncalcium ion binding
30005737cellular_componentcytoplasm
30010467biological_processgene expression
30030424cellular_componentaxon
30032420cellular_componentstereocilium
30032437cellular_componentcuticular plate
30032991cellular_componentprotein-containing complex
30042802molecular_functionidentical protein binding
30043025cellular_componentneuronal cell body
30043195cellular_componentterminal bouton
30044877molecular_functionprotein-containing complex binding
30046872molecular_functionmetal ion binding
30090102biological_processcochlea development
30098976biological_processexcitatory chemical synaptic transmission
30098977biological_processinhibitory chemical synaptic transmission
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA 1 110
ChainResidue
1ASP51
1ASP53
1SER55
1PHE57
1GLU59
1GLU62

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA 1 111
ChainResidue
1ASP90
1ASP92
1ASP94
1LYS96
1GLU101
1HOH121

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA 2 110
ChainResidue
2ASP51
2ASP53
2SER55
2PHE57
2GLU59
2GLU62

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA 2 111
ChainResidue
2ASP90
2ASP92
2ASP94
2LYS96
2GLU101
2HOH148

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA 3 110
ChainResidue
3ASP51
3ASP53
3SER55
3PHE57
3GLU59
3GLU62

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA 3 111
ChainResidue
3ASP90
3ASP92
3ASP94
3LYS96
3GLU101
3HOH145

site_idCA1
Number of Residues6
Details
ChainResidue
1ASP51
1ASP53
1SER55
1PHE57
1GLU59
1GLU62

site_idCA2
Number of Residues6
Details
ChainResidue
1LYS96
1GLU101
1HOH121
1ASP90
1ASP92
1ASP94

site_idCB1
Number of Residues6
Details
ChainResidue
2ASP51
2ASP53
2SER55
2PHE57
2GLU59
2GLU62

site_idCB2
Number of Residues6
Details
ChainResidue
2ASP90
2ASP92
2ASP94
2LYS96
2GLU101
1HOH121

site_idCC1
Number of Residues6
Details
ChainResidue
3ASP51
3ASP53
3SER55
3PHE57
3GLU59
3GLU62

site_idCC2
Number of Residues6
Details
ChainResidue
3ASP90
3ASP92
3ASP94
3LYS96
3GLU101
1HOH121

Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DKDKSGFIEedEL
ChainResidueDetails
1ASP51-LEU63
1ASP90-PHE102

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues27
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448
ChainResidueDetails
1LYS52
2LYS52
2LYS54
2GLY56
2LEU63
2LYS91
2GLY93
2GLY95
2ILE97
2PHE102
3LYS52
1LYS54
3LYS54
3GLY56
3LEU63
3LYS91
3GLY93
3GLY95
3ILE97
3PHE102
1GLY56
1LEU63
1LYS91
1GLY93
1GLY95
1ILE97
1PHE102

site_idSWS_FT_FI2
Number of Residues12
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903
ChainResidueDetails
1MET2
3ALA8
3PHE24
3ILE66
1ALA8
1PHE24
1ILE66
2MET2
2ALA8
2PHE24
2ILE66
3MET2

218853

PDB entries from 2024-04-24

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