eF-site ID 6cwy-D PDB Code 6cwy Chain D click to enlarge Title Crystal structure of SUMO E1 in complex with an allosteric inhibitor Classification transferase/transferase inhibitor Compound SUMO-activating enzyme subunit 1 Source (SAE2_HUMAN) Sequence D:  LSRGLPRELAEAVAGGRVLVVGAGGIGCELLKNLVLTGFS HIDLIDLDTIDGRSKAQVAKESVLQFYPKANIVAYHDSIM NPDYNVEFFRQFILVMNALDNRAARNHVNRMCLAADVPLI ESGTAGYLGQVTTIKKGVTECYECHPKPTQRTFPGCTIRN TPSEPIHCIVWAKYLFNQLFGEEDADQEVSPDRADPEAAW EPTEAEAISTKEWAKSTGYDPVKLFTKLFKDDIRYLLTMD KLWRKRKPPVPLDWAEVQSQLDVKSYARLFSKSIETLRVH LIWDKDDPSAMDFVTSAANLRMHIFSMNMKSRFDIKSMAG NIIPAIATTNAVIAGLIVLEGLKILSGKIDQCRTIFLNKQ PNPRKKLLVPCALDPPNPNCYVCASKPEVTVRLNVHKVTV LTLQDKIVKEKFAMVAPDVQIEDGKGTILISSEEGETEAN NHKKLSEFGIRNGSRLQADDFLQDYTLLINILHSEDLGKD VEFEVVG Description Functional site 1) chain D residue 158 type sequence C description binding site for residue ZN D 701 source : AC3 2) chain D residue 161 type sequence C description binding site for residue ZN D 701 source : AC3 3) chain D residue 441 type sequence C description binding site for residue ZN D 701 source : AC3 4) chain D residue 444 type sequence C description binding site for residue ZN D 701 source : AC3 5) chain D residue 96 type sequence I description binding site for residue MG D 702 source : AC4 6) chain D residue 98 type sequence N description binding site for residue MG D 702 source : AC4 7) chain D residue 101 type sequence Y description binding site for residue MG D 702 source : AC4 8) chain D residue 124 type sequence H description binding site for residue MG D 702 source : AC4 9) chain D residue 176 type sequence R description binding site for residue SO4 D 703 source : AC5 10) chain D residue 205 type sequence E description binding site for residue SO4 D 703 source : AC5 11) chain D residue 208 type sequence P description binding site for residue SO4 D 703 source : AC5 12) chain D residue 209 type sequence D description binding site for residue SO4 D 703 source : AC5 13) chain D residue 210 type sequence R description binding site for residue SO4 D 703 source : AC5 14) chain D residue 211 type sequence A description binding site for residue SO4 D 703 source : AC5 15) chain D residue 119 type sequence R description binding site for residue SO4 D 704 source : AC6 16) chain D residue 165 type sequence P description binding site for residue SO4 D 704 source : AC6 17) chain D residue 166 type sequence T description binding site for residue SO4 D 704 source : AC6 18) chain D residue 168 type sequence R description binding site for residue SO4 D 704 source : AC6 19) chain D residue 378 type sequence S description binding site for residue SO4 D 704 source : AC6 20) chain D residue 74 type sequence Q description binding site for residue SO4 D 705 source : AC7 21) chain D residue 77 type sequence K description binding site for residue SO4 D 705 source : AC7 22) chain D residue 91 type sequence A description binding site for residue SO4 D 705 source : AC7 23) chain D residue 417 type sequence F description binding site for residue SO4 D 706 source : AC8 24) chain D residue 419 type sequence N description binding site for residue SO4 D 706 source : AC8 25) chain D residue 430 type sequence V description binding site for residue SO4 D 706 source : AC8 26) chain D residue 30 type sequence C description binding site for residue FHJ D 707 source : AC9 27) chain D residue 31 type sequence E description binding site for residue FHJ D 707 source : AC9 28) chain D residue 34 type sequence K description binding site for residue FHJ D 707 source : AC9 29) chain D residue 76 type sequence A description binding site for residue FHJ D 707 source : AC9 30) chain D residue 79 type sequence S description binding site for residue FHJ D 707 source : AC9 31) chain D residue 80 type sequence V description binding site for residue FHJ D 707 source : AC9 32) chain D residue 83 type sequence F description binding site for residue FHJ D 707 source : AC9 33) chain D 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 34) chain D residue 190 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) source Swiss-Prot : SWS_FT_FI10 35) chain D residue 275 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) source Swiss-Prot : SWS_FT_FI10 36) chain D residue 24 type BINDING sequence G description BINDING => ECO:0000269|PubMed:15660128 source Swiss-Prot : SWS_FT_FI2 37) chain D residue 48 type BINDING sequence D description BINDING => ECO:0000269|PubMed:15660128 source Swiss-Prot : SWS_FT_FI2 38) chain D residue 72 type BINDING sequence K description BINDING => ECO:0000269|PubMed:15660128 source Swiss-Prot : SWS_FT_FI2 39) chain D residue 95 type BINDING sequence S description BINDING => ECO:0000269|PubMed:15660128 source Swiss-Prot : SWS_FT_FI2 40) chain D residue 117 type BINDING sequence D description BINDING => ECO:0000269|PubMed:15660128 source Swiss-Prot : SWS_FT_FI2 41) chain D residue 158 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI3 42) chain D residue 161 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI3 43) chain D residue 441 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI3 44) chain D residue 444 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI3 45) chain D residue 271 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI5 46) chain D residue 207 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI4 47) chain D 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 48) chain D 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 49) chain D 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 50) chain D 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 51) chain D 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 52) chain D residue 507 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 53) chain D 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 54) chain D residue 404-412 type prosite sequence KILSGKIDQ description UBIQUITIN_ACTIVAT_1 Ubiquitin-activating enzyme signature 1. KILSGKIdQ source prosite : PS00536 55) chain D residue 171-179 type prosite sequence PGCTIRNTP description UBIQUITIN_ACTIVAT_2 Ubiquitin-activating enzyme active site. PGCTIRnTP source prosite : PS00865

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