eF-site ID 1he8-AB PDB Code 1he8 Chain A, B click to enlarge Title Ras G12V - PI 3-kinase gamma complex Classification KINASE/HYDROLASE Compound PHOSPHATIDYLINOSITOL 3-KINASE CATALYTIC SUBUNIT, GAMMA ISOFORM Source (RASH_MSVNS) Sequence A:  SEESQAFQRQLTALIGYDVTDVSNVHDDELEFTRRGLVTP RMAEVASRDPKLYAMHPWVTSKPLPEYLWKKIANNCIFIK IHRSTTSQTIKVSPDDTPGAILQSFFTKMAKKKSLMDIPE SQSEQDFVLRVCGRDEYLVGETPIKNFQWVRHCLKNGEEI HVVLDTPPDPALDEVRKESLWDCDRKFRVKIRGIDIPVLP LTVFVEANIQHGQQVLCQRRTSPKPFTEEVLWNVWLEFSI KIKDLPKGALLNLQIYCKVRLLYYVNLLLIDHRFLLRRGE YVLHMWQISNADKLTSATNPDKENSMSISILLDNYCHPIS ALDVGLTMQLLDCNFSDENVRAIAVQKLESLEDDDVLHYL LQLVQAVKFEPYHDSALARFLLKRGLRNKRIGHFLFWFLR SEIAQSRHYQQRFAVILEAYLRGCGTAMLHDFTQQVQVIE MLQKVTLDIKSLSSQVISQLKQKLENLQNSQLPESFRVPY DPGLKAGALAIEKCKVMASKKKPLWLEFKCADPTALSNET IGIIFKHGDDLRQDMLILQILRIMESIWETESLDLCLLPY GCISTGDKIGMIEIVKDATTIAKIQQSTFKDEVLNHWLKE KSPTEEKFQAAVERFVYSCAGYCVATFVLGIGDRHNDNIM ITETGNLFHIDFGHERVPFVLTPDFLFVMGTSGKKTSPHF QKFQDICVKAYLALRHHTNLLIILFSMMLMTDIEYIRDAL TVGKNEEDAKKYFLDQIEVCRDKGWTVQF B:  MTEYKLVVVGAVGVGKSALTIQLIQNHFVDEYDPTIEDSY RKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLC VFAINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDL AARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLV REIRQH Description Functional site 1) chain B residue 17 type sequence S description BINDING SITE FOR RESIDUE MG C 1 source : AC1 2) chain B residue 35 type sequence T description BINDING SITE FOR RESIDUE MG C 1 source : AC1 3) chain A residue 647 type sequence K description BINDING SITE FOR RESIDUE GNP C 2 source : AC2 4) chain B residue 11 type sequence A description BINDING SITE FOR RESIDUE GNP C 2 source : AC2 5) chain B residue 12 type sequence V description BINDING SITE FOR RESIDUE GNP C 2 source : AC2 6) chain B residue 13 type sequence G description BINDING SITE FOR RESIDUE GNP C 2 source : AC2 7) chain B residue 14 type sequence V description BINDING SITE FOR RESIDUE GNP C 2 source : AC2 8) chain B residue 15 type sequence G description BINDING SITE FOR RESIDUE GNP C 2 source : AC2 9) chain B residue 16 type sequence K description BINDING SITE FOR RESIDUE GNP C 2 source : AC2 10) chain B residue 17 type sequence S description BINDING SITE FOR RESIDUE GNP C 2 source : AC2 11) chain B residue 18 type sequence A description BINDING SITE FOR RESIDUE GNP C 2 source : AC2 12) chain B residue 28 type sequence F description BINDING SITE FOR RESIDUE GNP C 2 source : AC2 13) chain B residue 29 type sequence V description BINDING SITE FOR RESIDUE GNP C 2 source : AC2 14) chain B residue 30 type sequence D description BINDING SITE FOR RESIDUE GNP C 2 source : AC2 15) chain B residue 32 type sequence Y description BINDING SITE FOR RESIDUE GNP C 2 source : AC2 16) chain B residue 34 type sequence P description BINDING SITE FOR RESIDUE GNP C 2 source : AC2 17) chain B residue 35 type sequence T description BINDING SITE FOR RESIDUE GNP C 2 source : AC2 18) chain B residue 60 type sequence G description BINDING SITE FOR RESIDUE GNP C 2 source : AC2 19) chain B residue 116 type sequence N description BINDING SITE FOR RESIDUE GNP C 2 source : AC2 20) chain B residue 117 type sequence K description BINDING SITE FOR RESIDUE GNP C 2 source : AC2 21) chain B residue 119 type sequence D description BINDING SITE FOR RESIDUE GNP C 2 source : AC2 22) chain B residue 120 type sequence L description BINDING SITE FOR RESIDUE GNP C 2 source : AC2 23) chain B residue 145 type sequence S description BINDING SITE FOR RESIDUE GNP C 2 source : AC2 24) chain B residue 146 type sequence A description BINDING SITE FOR RESIDUE GNP C 2 source : AC2 25) chain B residue 10 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI1 26) chain B residue 57 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI1 27) chain A residue 962 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI1 28) chain B residue 35 type CARBOHYD sequence T description (Microbial infection) O-linked (Glc) threonine; by P.sordellii toxin TcsL => ECO:0000269|PubMed:19744486, ECO:0000269|PubMed:8626575, ECO:0000269|PubMed:8626586, ECO:0000269|PubMed:9632667 source Swiss-Prot : SWS_FT_FI6 29) chain B residue 2 type MOD_RES sequence T description N-acetylthreonine; in GTPase HRas, N-terminally processed => ECO:0000269|Ref.12 source Swiss-Prot : SWS_FT_FI4 30) chain B residue 118 type MOD_RES sequence C description S-nitrosocysteine => ECO:0000269|PubMed:9020151 source Swiss-Prot : SWS_FT_FI5 31) chain A residue 832-846 type prosite sequence FKHGDDLRQDMLILQ description PI3_4_KINASE_1 Phosphatidylinositol 3- and 4-kinases signature 1. FKhg.DDLRQDmlilQ source prosite : PS00915 32) chain A residue 931-951 type prosite sequence SCAGYCVATFVLGIGDRHNDN description PI3_4_KINASE_2 Phosphatidylinositol 3- and 4-kinases signature 2. ScAgycVatFVLgIgDRHndN source prosite : PS00916 33) chain B residue 116 type BINDING sequence N description BINDING => ECO:0000269|PubMed:16698776 source Swiss-Prot : SWS_FT_FI2 34) chain B residue 13 type BINDING sequence G description BINDING => ECO:0000269|PubMed:16698776 source Swiss-Prot : SWS_FT_FI2 35) chain B residue 29 type BINDING sequence V description BINDING => ECO:0000269|PubMed:16698776 source Swiss-Prot : SWS_FT_FI2 36) chain B residue 59 type BINDING sequence A description BINDING => ECO:0000269|PubMed:16698776 source Swiss-Prot : SWS_FT_FI2 37) chain B residue 145 type BINDING sequence S description BINDING => ECO:0000269|PubMed:16698776 source Swiss-Prot : SWS_FT_FI2 38) chain B residue 1 type MOD_RES sequence M description N-acetylmethionine; in GTPase HRas; alternate => ECO:0000269|Ref.12 source Swiss-Prot : SWS_FT_FI3

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