eF-site ID 6qu1-A PDB Code 6qu1 Chain A click to enlarge Title Crystal structure of the KAP1 RBCC domain in complex with the SMARCAD1 CUE1 domain at 3.7 angstrom resolution. Classification LIGASE Compound Transcription intermediary factor 1-beta,Transcription intermediary factor 1-beta Source (SMRCD_HUMAN) Sequence A:  LELLEHCGVCRERLRPEREPRLLPCLHSACSACLGPTVVD CPVCKQQCFSKDIVENYFMRDCNVHKHEPLVLFCESCDTL TCRDCQLNAHKDHQYQFLEDAVRNQRKLLASLVKRLGDKH ATLQKSTKEVRSSIRQVSDVQKRVQVDVKMAILQIMKELN KRGRVLVNDAQKVTEGQQERLERQHWTMTKIQKHQEHILR FASWALESDNNTALLLSKKLIYFQLHRALKMIVDPVEPHG EMKFQWDLNAWTKSAEAFGKIV Description Functional site 1) chain A residue 65 type sequence C description binding site for residue ZN A 1001 source : AC1 2) chain A residue 66 type sequence G description binding site for residue ZN A 1001 source : AC1 3) chain A residue 68 type sequence C description binding site for residue ZN A 1001 source : AC1 4) chain A residue 88 type sequence C description binding site for residue ZN A 1001 source : AC1 5) chain A residue 91 type sequence C description binding site for residue ZN A 1001 source : AC1 6) chain A residue 83 type sequence C description binding site for residue ZN A 1002 source : AC2 7) chain A residue 85 type sequence H description binding site for residue ZN A 1002 source : AC2 8) chain A residue 117 type sequence C description binding site for residue ZN A 1002 source : AC2 9) chain A residue 120 type sequence C description binding site for residue ZN A 1002 source : AC2 10) chain A residue 209 type sequence C description binding site for residue ZN A 1003 source : AC3 11) chain A residue 212 type sequence H description binding site for residue ZN A 1003 source : AC3 12) chain A residue 229 type sequence C description binding site for residue ZN A 1003 source : AC3 13) chain A residue 232 type sequence C description binding site for residue ZN A 1003 source : AC3 14) chain A residue 221 type sequence C description binding site for residue ZN A 1004 source : AC4 15) chain A residue 223 type sequence S description binding site for residue ZN A 1004 source : AC4 16) chain A residue 224 type sequence C description binding site for residue ZN A 1004 source : AC4 17) chain A residue 237 type sequence H description binding site for residue ZN A 1004 source : AC4 18) chain A residue 240 type sequence H description binding site for residue ZN A 1004 source : AC4 19) chain A residue 259 type CROSSLNK sequence L description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI10 20) chain A residue 254 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI10 21) chain A residue 261 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI10 22) chain A residue 319 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI10 23) chain A residue 213 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00024 source Swiss-Prot : SWS_FT_FI4 24) chain A residue 216 type BINDING sequence P description BINDING => ECO:0000255|PROSITE-ProRule:PRU00024 source Swiss-Prot : SWS_FT_FI4 25) chain A residue 237 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00024 source Swiss-Prot : SWS_FT_FI4 26) chain A residue 241 type BINDING sequence Q description BINDING => ECO:0000255|PROSITE-ProRule:PRU00024 source Swiss-Prot : SWS_FT_FI4 27) chain A residue 209 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00024 source Swiss-Prot : SWS_FT_FI4 28) chain A residue 212 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00024 source Swiss-Prot : SWS_FT_FI4 29) chain A residue 232 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00024 source Swiss-Prot : SWS_FT_FI4 30) chain A residue 304 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_FI11 31) chain A residue 366 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25218447 source Swiss-Prot : SWS_FT_FI12 32) chain A residue 377 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI13 33) chain A residue 266 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:Q62318 source Swiss-Prot : SWS_FT_FI6 34) chain A residue 304 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 35) chain A residue 377 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 36) chain A residue 340 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI8 37) chain A residue 127 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_FI9 38) chain A residue 272 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_FI9 39) chain A residue 407 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_FI9

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