eF-site ID 5dyl-A PDB Code 5dyl Chain A click to enlarge Title Crystal structure of the cGMP-dependent protein kinase PKG from Plasmodium Vivax - Apo form Classification TRANSFERASE Compound cGMP-dependent protein kinase, putative Source (A5K0N4_PLAVS) Sequence A:  GMRCNEKKKAIFGEDTLMEDHLQLREKLSEDIEMIKASLK NNLVCSTLNDNEILTLSNYMQFFVFKGGDLVIKQGEKGSY FFIINSGKFDVYVNDKKVKSMGKGSSFGEAALIHNTQRSA TIMAETDGTLWGVQRSTFRATLKQLSNRNFNENRSFIDSV SVFDMLTEAQKNMITNACVIQMFKPGETIVKQGDYGDVLF ILKEGKATVFINDKEIRVLNKGSYFGERALLYDEPRSATI IAKEPTACASICRKLLNIVLGNLQVVLFRNIMTEALQQSE IFRQFSAEQLNDLADTAIVRDYPANYHILHKKSVKYLIVL EGKVELFLDDESIGILTRGKSFGDQYVLNQKQKFRHTVKS LDVCKIALITESCLADCLGDNNIDASIDHNNKKSIIKKMY IFRYLSEQQCNLLIEAFRTTRYEEGDYIIQEGEVGSRFYI IKNGEVEVTKNKRLRTLGKNDYFGERALLYDEPRTASIIS KATSVECWFVDKSVFLQIIQGPMLTHLEERIKMQDTKVEM HELETERIIGRGFGTVKLVHHKPTQIRYALKCVSKRSIIS LNQQNNIKLEREITAENDHPFIIRLVRTFKDCFYFLTELV TGGELYDAIRKLGLLSKPQAQFYLGSIILAIEYLHERNIV YRDLKPENILLDKQGYVKLIDFGCAKKIQGRAYTLVGTPH YMAPEVILGKGYGCTVDIWALGVCLYEFICGPLPFGNDQE DQLEIFRDILTGQLTFPDYVSDQDSINLMKRLLCRLPQGR IGCSINGFKDIKEHAFFGNFNWDKLAGRLLEPPLVSKGET YA Description Functional site 1) chain A residue 540-563 type prosite sequence IGRGFGTVKLVHHKPTQIRYALK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGRGTFGTVKlVhhkptqir..........YALK source prosite : PS00107 2) chain A residue 653-665 type prosite sequence IVYRDLKPENILL description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvYrDLKpeNILL source prosite : PS00108 3) chain A residue 78-94 type prosite sequence VIKQGEKGSYFFIINSG description CNMP_BINDING_1 Cyclic nucleotide-binding domain signature 1. VIkQGEkGSyFFIInsG source prosite : PS00888 4) chain A residue 196-212 type prosite sequence IVKQGDYGDVLFILKEG description CNMP_BINDING_1 Cyclic nucleotide-binding domain signature 1. VIkQGEkGSyFFIInsG source prosite : PS00888 5) chain A residue 438-454 type prosite sequence IIQEGEVGSRFYIIKNG description CNMP_BINDING_1 Cyclic nucleotide-binding domain signature 1. VIkQGEkGSyFFIInsG source prosite : PS00888 6) chain A residue 114-131 type prosite sequence FGEAALIHNTQRSATIMA description CNMP_BINDING_2 Cyclic nucleotide-binding domain signature 2. FGEaALihntq......RSAtImA source prosite : PS00889 7) chain A residue 232-249 type prosite sequence FGERALLYDEPRSATIIA description CNMP_BINDING_2 Cyclic nucleotide-binding domain signature 2. FGEaALihntq......RSAtImA source prosite : PS00889 8) chain A residue 474-491 type prosite sequence FGERALLYDEPRTASIIS description CNMP_BINDING_2 Cyclic nucleotide-binding domain signature 2. FGEaALihntq......RSAtImA source prosite : PS00889 9) chain A residue 657 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI1 10) chain A residue 106 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:Q8I719 source Swiss-Prot : SWS_FT_FI2 11) chain A residue 478 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:Q8I719 source Swiss-Prot : SWS_FT_FI2 12) chain A residue 485 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:Q8I719 source Swiss-Prot : SWS_FT_FI2 13) chain A residue 486 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:Q8I719 source Swiss-Prot : SWS_FT_FI2 14) chain A residue 115 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q8I719 source Swiss-Prot : SWS_FT_FI2 15) chain A residue 116 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:Q8I719 source Swiss-Prot : SWS_FT_FI2 16) chain A residue 118 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:Q8I719 source Swiss-Prot : SWS_FT_FI2 17) chain A residue 125 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:Q8I719 source Swiss-Prot : SWS_FT_FI2 18) chain A residue 126 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:Q8I719 source Swiss-Prot : SWS_FT_FI2 19) chain A residue 466 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:Q8I719 source Swiss-Prot : SWS_FT_FI2 20) chain A residue 475 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q8I719 source Swiss-Prot : SWS_FT_FI2 21) chain A residue 476 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:Q8I719 source Swiss-Prot : SWS_FT_FI2 22) chain A residue 540 type BINDING sequence I description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI3 23) chain A residue 563 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:31239348, ECO:0007744|PDB:5DZC source Swiss-Prot : SWS_FT_FI4 24) chain A residue 477 type SITE sequence R description Part of a catalytic triad required for cGMP binding and cGMP-dependent kinase activity => ECO:0000250|UniProtKB:Q8I719 source Swiss-Prot : SWS_FT_FI5 25) chain A residue 525 type SITE sequence Q description Part of a catalytic triad required for cGMP binding and cGMP-dependent kinase activity => ECO:0000250|UniProtKB:Q8I719 source Swiss-Prot : SWS_FT_FI5 26) chain A residue 526 type SITE sequence D description Part of a catalytic triad required for cGMP binding and cGMP-dependent kinase activity => ECO:0000250|UniProtKB:Q8I719 source Swiss-Prot : SWS_FT_FI5

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