eF-site ID 3kyc-B PDB Code 3kyc Chain B click to enlarge Title Human SUMO E1 complex with a SUMO1-AMP mimic Classification LIGASE Compound SUMO-activating enzyme subunit 1 Source Homo sapiens (Human) (SUMO1_HUMAN) Sequence B:  RGLPRELAEAVAGGRVLVVGAGGIGCELLKNLVLTGFSHI DLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFY PKANIVAYHDSIMNPDYNVEFFRQFILVMNALDNRAARNH VNRMCLAADVPLIESGTAGYLGQVTTIKKGVTECYECHPK PTQRTFPGCTIRNTPSEPIHCIVWAKYLFNQLFGEEDADQ EVSPDRADPEAAWIKRISTKEWAKSTGYDPVKLFTKLFKD DIRYLLTMDKLWRKRKPPVPLDWAEVQSQGLGLKDQQVLD VKSYARLFSKSIETLRVHLAEKGDGAELIWDKDDPSAMDF VTSAANLRMHIFSMNMKSRFDIKSMAGNIIPAIATTNAVI AGLIVLEGLKILSGKIDQCRTIFLNKQPNPRKKLLVPCAL DPPNPNCYVCASKPEVTVRLNVHKVTVLTLQDKIVKEKFA MVAPDVQIEDGKGTILISSEEGETEANNHKKLSEFGIRNG SRLQADDFLQDYTLLINILHSEDLGKDVEFEVVGERSRKR KLDEKENLSAKRSRIEQKEELDDVIALD Description Functional site 1) chain B residue 158 type sequence C description BINDING SITE FOR RESIDUE ZN B 641 source : AC1 2) chain B residue 161 type sequence C description BINDING SITE FOR RESIDUE ZN B 641 source : AC1 3) chain B residue 441 type sequence C description BINDING SITE FOR RESIDUE ZN B 641 source : AC1 4) chain B residue 444 type sequence C description BINDING SITE FOR RESIDUE ZN B 641 source : AC1 5) chain B residue 26 type sequence G description BINDING SITE FOR RESIDUE JZU D 98 source : AC2 6) chain B residue 27 type sequence G description BINDING SITE FOR RESIDUE JZU D 98 source : AC2 7) chain B residue 48 type sequence D description BINDING SITE FOR RESIDUE JZU D 98 source : AC2 8) chain B residue 49 type sequence L description BINDING SITE FOR RESIDUE JZU D 98 source : AC2 9) chain B residue 50 type sequence D description BINDING SITE FOR RESIDUE JZU D 98 source : AC2 10) chain B residue 60 type sequence Q description BINDING SITE FOR RESIDUE JZU D 98 source : AC2 11) chain B residue 72 type sequence K description BINDING SITE FOR RESIDUE JZU D 98 source : AC2 12) chain B residue 94 type sequence D description BINDING SITE FOR RESIDUE JZU D 98 source : AC2 13) chain B residue 95 type sequence S description BINDING SITE FOR RESIDUE JZU D 98 source : AC2 14) chain B residue 96 type sequence I description BINDING SITE FOR RESIDUE JZU D 98 source : AC2 15) chain B residue 97 type sequence M description BINDING SITE FOR RESIDUE JZU D 98 source : AC2 16) chain B residue 115 type sequence A description BINDING SITE FOR RESIDUE JZU D 98 source : AC2 17) chain B residue 116 type sequence L description BINDING SITE FOR RESIDUE JZU D 98 source : AC2 18) chain B residue 117 type sequence D description BINDING SITE FOR RESIDUE JZU D 98 source : AC2 19) chain B residue 118 type sequence N description BINDING SITE FOR RESIDUE JZU D 98 source : AC2 20) chain B residue 121 type sequence A description BINDING SITE FOR RESIDUE JZU D 98 source : AC2 21) chain B residue 257 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI12 22) chain B residue 420 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI12 23) chain B residue 271 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate source Swiss-Prot : SWS_FT_FI13 24) chain B residue 613 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate source Swiss-Prot : SWS_FT_FI13 25) chain B residue 371 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI14 26) chain B residue 540 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI14 27) chain B residue 404-412 type prosite sequence KILSGKIDQ description UBIQUITIN_ACTIVAT_1 Ubiquitin-activating enzyme signature 1. KILSGKIdQ source prosite : PS00536 28) chain B residue 171-179 type prosite sequence PGCTIRNTP description UBIQUITIN_ACTIVAT_2 Ubiquitin-activating enzyme active site. PGCTIRnTP source prosite : PS00865 29) chain B residue 24 type BINDING sequence G description BINDING => ECO:0000269|PubMed:15660128 source Swiss-Prot : SWS_FT_FI2 30) chain B residue 48 type BINDING sequence D description BINDING => ECO:0000269|PubMed:15660128 source Swiss-Prot : SWS_FT_FI2 31) chain B residue 56 type BINDING sequence N description BINDING => ECO:0000269|PubMed:15660128 source Swiss-Prot : SWS_FT_FI2 32) chain B residue 72 type BINDING sequence K description BINDING => ECO:0000269|PubMed:15660128 source Swiss-Prot : SWS_FT_FI2 33) chain B residue 95 type BINDING sequence S description BINDING => ECO:0000269|PubMed:15660128 source Swiss-Prot : SWS_FT_FI2 34) chain B residue 117 type BINDING sequence D description BINDING => ECO:0000269|PubMed:15660128 source Swiss-Prot : SWS_FT_FI2 35) chain B residue 236 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI11 36) chain B residue 207 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI4 37) chain B residue 271 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI5 38) chain B residue 158 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI3 39) chain B residue 161 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI3 40) chain B residue 441 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI3 41) chain B residue 444 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI3 42) chain B residue 173 type ACT_SITE sequence C description Glycyl thioester intermediate => ECO:0000255|PROSITE-ProRule:PRU10132, ECO:0000269|PubMed:15660128, ECO:0000269|PubMed:20164921 source Swiss-Prot : SWS_FT_FI1 43) chain B residue 507 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 44) chain B residue 613 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:Q9Z1F9 source Swiss-Prot : SWS_FT_FI8 45) chain B residue 164 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) => ECO:0007744|PubMed:25114211 source Swiss-Prot : SWS_FT_FI9 46) chain B residue 190 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) source Swiss-Prot : SWS_FT_FI10 47) chain B residue 275 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) source Swiss-Prot : SWS_FT_FI10 48) chain B residue 611 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) source Swiss-Prot : SWS_FT_FI10 49) chain B residue 617 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) source Swiss-Prot : SWS_FT_FI10 50) chain B residue 623 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) source Swiss-Prot : SWS_FT_FI10

Display surface Download Links