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2GGZ

Crystal Structure of Human Guanylate Cyclase Activating Protein-3

Functional Information from GO Data
ChainGOidnamespacecontents
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0007165biological_processsignal transduction
A0007601biological_processvisual perception
A0008048molecular_functioncalcium sensitive guanylate cyclase activator activity
A0046872molecular_functionmetal ion binding
A0097381cellular_componentphotoreceptor disc membrane
B0005509molecular_functioncalcium ion binding
B0005515molecular_functionprotein binding
B0007165biological_processsignal transduction
B0007601biological_processvisual perception
B0008048molecular_functioncalcium sensitive guanylate cyclase activator activity
B0046872molecular_functionmetal ion binding
B0097381cellular_componentphotoreceptor disc membrane
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 500
ChainResidue
AASP64
AASN66
AASP68
APHE70
AASP72
AGLU75

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 501
ChainResidue
ASER106
AGLU111
AASP100
AASP102
AASN104

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 502
ChainResidue
AASP142
AASN144
AASP146
AGLU148
AGLU153

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 503
ChainResidue
BASP64
BASN66
BASP68
BPHE70
BGLU75

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 504
ChainResidue
BASP100
BASP102
BASN104
BSER106
BGLU111

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 505
ChainResidue
BASP142
BASN144
BASP146
BGLU148
BGLU153

Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DTNKDGFVDflEF
ChainResidueDetails
AASP64-PHE76
AASP100-LEU112
AASP142-PHE154

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues28
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:16626734
ChainResidueDetails
ATHR65
ALYS67
AGLY69
APHE76
ALEU112
AILE143
AASN145
AGLY147
ALEU149
APHE154
BTHR65
BLYS67
BGLY69
BPHE76
BALA101
BGLY103
BGLY105
BILE107
BLEU112
BILE143
BASN145
BGLY147
BLEU149
BPHE154
AALA101
AGLY103
AGLY105
AILE107

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Deamidated asparagine => ECO:0000255
ChainResidueDetails
AGLY3
BGLY3

site_idSWS_FT_FI3
Number of Residues2
DetailsLIPID: N-myristoyl glycine => ECO:0000269|PubMed:10037746
ChainResidueDetails
AASN2
BASN2

221051

PDB entries from 2024-06-12

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