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6BDL

Crystal structure of cGMP-dependent protein kinase Ialpha (PKG Ialpha) catalytic domain in apo state

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0004692molecular_functioncGMP-dependent protein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0004674molecular_functionprotein serine/threonine kinase activity
B0004692molecular_functioncGMP-dependent protein kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue IMD A 700
ChainResidue
ALEU366
AALA388
AGLU439
ACYS441
AILE491

site_idAC2
Number of Residues4
Detailsbinding site for residue IMD B 700
ChainResidue
BALA388
BGLU439
BCYS441
BILE491

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues25
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGVGGFGRVElVqlkseeskt.........FAMK
ChainResidueDetails
ALEU366-LYS390

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiYrDLKpeNLIL
ChainResidueDetails
AILE480-LEU492

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:21526164, ECO:0007744|PDB:3OD0
ChainResidueDetails
AILE449
ASER459
BILE449
BSER459

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:24239458, ECO:0000269|PubMed:25271401, ECO:0007744|PDB:4KU7, ECO:0007744|PDB:4QXK
ChainResidueDetails
AMET564
AGLY573
AILE583
ATRP618
BMET564
BGLY573
BILE583
BTRP618

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AASN648
BASN648

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by autocatalysis => ECO:0000250|UniProtKB:P00516
ChainResidueDetails
AALA341
BALA341

223790

PDB entries from 2024-08-14

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