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4PNI

Bovine G protein-coupled receptor kinase 1 in complex with GSK2163632A

Functional Information from GO Data
ChainGOidnamespacecontents
A0001750cellular_componentphotoreceptor outer segment
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0004703molecular_functionG protein-coupled receptor kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006468biological_processprotein phosphorylation
A0007165biological_processsignal transduction
A0007601biological_processvisual perception
A0009966biological_processregulation of signal transduction
A0016020cellular_componentmembrane
A0022400biological_processregulation of opsin-mediated signaling pathway
A0042995cellular_componentcell projection
A0046777biological_processprotein autophosphorylation
A0050254molecular_functionrhodopsin kinase activity
A0097381cellular_componentphotoreceptor disc membrane
Functional Information from PDB Data
site_idAC1
Number of Residues11
Detailsbinding site for residue KQQ A 601
ChainResidue
ALEU193
AARG474
ATHR475
APHE198
AALA214
ATHR265
AMET267
AASN268
AGLY270
AASP271
ALEU321

site_idAC2
Number of Residues3
Detailsbinding site for residue CL A 602
ChainResidue
ALEU166
AARG170
AGLN173

site_idAC3
Number of Residues2
Detailsbinding site for residue CL A 603
ChainResidue
AGLN287
AARG290

site_idAC4
Number of Residues4
Detailsbinding site for residue CL A 604
ChainResidue
AARG386
APHE389
AGLN408
AARG453

site_idAC5
Number of Residues2
Detailsbinding site for residue CL A 605
ChainResidue
ATRP457
AARG458

site_idAC6
Number of Residues5
Detailsbinding site for residue CL A 606
ChainResidue
AGLY387
APRO388
APHE389
AARG390
AHOH846

site_idAC7
Number of Residues1
Detailsbinding site for residue CL A 607
ChainResidue
ALYS90

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGRGGFGEVFaCqmkatgkl..........YACK
ChainResidueDetails
ALEU193-LYS216

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiYrDLKpeNVLL
ChainResidueDetails
AILE310-LEU322

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP314

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:18339619
ChainResidueDetails
ALEU193

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALYS216

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:18339619
ChainResidueDetails
ATHR265
AASP332

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:18339619
ChainResidueDetails
ASER5

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:18339619
ChainResidueDetails
ATHR8

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PKA and autocatalysis => ECO:0000305|PubMed:1527025, ECO:0000305|PubMed:18339619
ChainResidueDetails
ASER21

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:1527025, ECO:0000269|PubMed:18339619
ChainResidueDetails
ASER488

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:1527025, ECO:0000269|PubMed:18339619
ChainResidueDetails
ATHR489

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Cysteine methyl ester => ECO:0000269|PubMed:1730692
ChainResidueDetails
ACYS558

site_idSWS_FT_FI11
Number of Residues1
DetailsLIPID: S-farnesyl cysteine => ECO:0000269|PubMed:1730692
ChainResidueDetails
ACYS558

223532

PDB entries from 2024-08-07

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