eF-site ID 1qg2-A PDB Code 1qg2 Chain A click to enlarge Title CANINE GDP-RAN R76E MUTANT Classification GTPASE Compound PROTEIN (RAN) Source null (RAN_CANFA) Sequence A:  QVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEV HPLVFHTNRGPIKFNVWDTAGQEKFGGLEDGYYIQAQCAI IMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLCGNKVDIK DRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARK LIGDPNLEFVAMPALAPPEVVMDPALAAQYEHDLEVAQTT A Description Functional site 1) chain A residue 24 type sequence T description BINDING SITE FOR RESIDUE MG A 221 source : AC1 2) chain A residue 18 type sequence D description BINDING SITE FOR RESIDUE GDP A 220 source : AC2 3) chain A residue 20 type sequence G description BINDING SITE FOR RESIDUE GDP A 220 source : AC2 4) chain A residue 21 type sequence T description BINDING SITE FOR RESIDUE GDP A 220 source : AC2 5) chain A residue 22 type sequence G description BINDING SITE FOR RESIDUE GDP A 220 source : AC2 6) chain A residue 23 type sequence K description BINDING SITE FOR RESIDUE GDP A 220 source : AC2 7) chain A residue 24 type sequence T description BINDING SITE FOR RESIDUE GDP A 220 source : AC2 8) chain A residue 25 type sequence T description BINDING SITE FOR RESIDUE GDP A 220 source : AC2 9) chain A residue 122 type sequence N description BINDING SITE FOR RESIDUE GDP A 220 source : AC2 10) chain A residue 123 type sequence K description BINDING SITE FOR RESIDUE GDP A 220 source : AC2 11) chain A residue 125 type sequence D description BINDING SITE FOR RESIDUE GDP A 220 source : AC2 12) chain A residue 150 type sequence S description BINDING SITE FOR RESIDUE GDP A 220 source : AC2 13) chain A residue 151 type sequence A description BINDING SITE FOR RESIDUE GDP A 220 source : AC2 14) chain A residue 152 type sequence K description BINDING SITE FOR RESIDUE GDP A 220 source : AC2 15) chain A residue 152 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0000250|UniProtKB:P62826 source Swiss-Prot : SWS_FT_FI11 16) chain A residue 69 type SITE sequence Q description Essential for GTP hydrolysis => ECO:0000250|UniProtKB:P62826 source Swiss-Prot : SWS_FT_FI4 17) chain A residue 24 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P62826 source Swiss-Prot : SWS_FT_FI6 18) chain A residue 60 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P62826 source Swiss-Prot : SWS_FT_FI7 19) chain A residue 99 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P62826 source Swiss-Prot : SWS_FT_FI7 20) chain A residue 134 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P62826 source Swiss-Prot : SWS_FT_FI7 21) chain A residue 37 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P62826 source Swiss-Prot : SWS_FT_FI7 22) chain A residue 71 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P62826 source Swiss-Prot : SWS_FT_FI8 23) chain A residue 159 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62827 source Swiss-Prot : SWS_FT_FI9 24) chain A residue 71 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62826 source Swiss-Prot : SWS_FT_FI10 25) chain A residue 18 type BINDING sequence D description BINDING => ECO:0000269|PubMed:15602554, ECO:0000269|PubMed:15864302, ECO:0000269|PubMed:19965479, ECO:0000269|PubMed:9533885, ECO:0000269|PubMed:9878368, ECO:0007744|PDB:1BYU, ECO:0007744|PDB:1WA5, ECO:0007744|PDB:2BKU, ECO:0007744|PDB:3A6P, ECO:0007744|PDB:3RAN, ECO:0007744|PDB:3W3Z, ECO:0007744|PDB:5BXQ source Swiss-Prot : SWS_FT_FI1 26) chain A residue 122 type BINDING sequence N description BINDING => ECO:0000269|PubMed:15602554, ECO:0000269|PubMed:15864302, ECO:0000269|PubMed:19965479, ECO:0000269|PubMed:9533885, ECO:0000269|PubMed:9878368, ECO:0007744|PDB:1BYU, ECO:0007744|PDB:1WA5, ECO:0007744|PDB:2BKU, ECO:0007744|PDB:3A6P, ECO:0007744|PDB:3RAN, ECO:0007744|PDB:3W3Z, ECO:0007744|PDB:5BXQ source Swiss-Prot : SWS_FT_FI1 27) chain A residue 150 type BINDING sequence S description BINDING => ECO:0000269|PubMed:15602554, ECO:0000269|PubMed:15864302, ECO:0000269|PubMed:19965479, ECO:0000269|PubMed:9533885, ECO:0000269|PubMed:9878368, ECO:0007744|PDB:1BYU, ECO:0007744|PDB:1WA5, ECO:0007744|PDB:2BKU, ECO:0007744|PDB:3A6P, ECO:0007744|PDB:3RAN, ECO:0007744|PDB:3W3Z, ECO:0007744|PDB:5BXQ source Swiss-Prot : SWS_FT_FI1 28) chain A residue 36 type BINDING sequence E description BINDING => ECO:0000269|PubMed:15602554, ECO:0000269|PubMed:15864302, ECO:0000269|PubMed:19965479, ECO:0007744|PDB:1WA5, ECO:0007744|PDB:2BKU, ECO:0007744|PDB:3A6P, ECO:0007744|PDB:3W3Z source Swiss-Prot : SWS_FT_FI2 29) chain A residue 68 type BINDING sequence G description BINDING => ECO:0000269|PubMed:15602554, ECO:0000269|PubMed:15864302, ECO:0000269|PubMed:19965479, ECO:0007744|PDB:1WA5, ECO:0007744|PDB:2BKU, ECO:0007744|PDB:3W3Z source Swiss-Prot : SWS_FT_FI3

Display surface Download Links