eF-site ID 1pdw-CDEFGH PDB Code 1pdw Chain C, D, E, F, G, H click to enlarge Title Crystal structure of human DJ-1, P 1 21 1 space group Classification PROTEIN BINDING Compound DJ-1 Source Homo sapiens (Human) (PARK7_HUMAN) Sequence C:  ASKRALVILAKGAEEXETVIPVDVXRRAGIKVTVAGLAGK DPVQCSRDVVICPDASLEDAKKEGPYDVVVLPGGNLGAQN LSESAAVKEILKEQENRKGLIAAICAGPTALLAHEIGFGS KVTTHPLAKDKXXNGGHYTYSENRVEKDGLILTSRGPGTS FEFALAIVEALNGKEVAAQVKAPLVLK D:  ASKRALVILAKGAEEXETVIPVDVXRRAGIKVTVAGLAGK DPVQCSRDVVICPDASLEDAKKEGPYDVVVLPGGNLGAQN LSESAAVKEILKEQENRKGLIAAICAGPTALLAHEIGFGS KVTTHPLAKDKXXNGGHYTYSENRVEKDGLILTSRGPGTS FEFALAIVEALNGKEVAAQVKAPLVLK E:  ASKRALVILAKGAEEXETVIPVDVXRRAGIKVTVAGLAGK DPVQCSRDVVICPDASLEDAKKEGPYDVVVLPGGNLGAQN LSESAAVKEILKEQENRKGLIAAICAGPTALLAHEIGFGS KVTTHPLAKDKXXNGGHYTYSENRVEKDGLILTSRGPGTS FEFALAIVEALNGKEVAAQVKAPLVLKDL F:  ASKRALVILAKGAEEXETVIPVDVXRRAGIKVTVAGLAGK DPVQCSRDVVICPDASLEDAKKEGPYDVVVLPGGNLGAQN LSESAAVKEILKEQENRKGLIAAICAGPTALLAHEIGFGS KVTTHPLAKDKXXNGGHYTYSENRVEKDGLILTSRGPGTS FEFALAIVEALNGKEVAAQVKAPLVLK G:  ASKRALVILAKGAEEXETVIPVDVXRRAGIKVTVAGLAGK DPVQCSRDVVICPDASLEDAKKEGPYDVVVLPGGNLGAQN LSESAAVKEILKEQENRKGLIAAICAGPTALLAHEIGFGS KVTTHPLAKDKXXNGGHYTYSENRVEKDGLILTSRGPGTS FEFALAIVEALNGKEVAAQVKAPLVLKDLEH H:  ASKRALVILAKGAEEXETVIPVDVXRRAGIKVTVAGLAGK DPVQCSRDVVICPDASLEDAKKEGPYDVVVLPGGNLGAQN LSESAAVKEILKEQENRKGLIAAICAGPTALLAHEIGFGS KVTTHPLAKDKXXNGGHYTYSENRVEKDGLILTSRGPGTS FEFALAIVEALNGKEVAAQVKAPLVLK Description (1)  DJ-1 Functional site 1) chain C residue 1106 type ACT_SITE sequence C description Nucleophile => ECO:0000305|PubMed:20304780, ECO:0000305|PubMed:25416785 source Swiss-Prot : SWS_FT_FI1 2) chain D residue 1306 type ACT_SITE sequence C description Nucleophile => ECO:0000305|PubMed:20304780, ECO:0000305|PubMed:25416785 source Swiss-Prot : SWS_FT_FI1 3) chain E residue 2106 type ACT_SITE sequence C description Nucleophile => ECO:0000305|PubMed:20304780, ECO:0000305|PubMed:25416785 source Swiss-Prot : SWS_FT_FI1 4) chain F residue 2306 type ACT_SITE sequence C description Nucleophile => ECO:0000305|PubMed:20304780, ECO:0000305|PubMed:25416785 source Swiss-Prot : SWS_FT_FI1 5) chain G residue 3106 type ACT_SITE sequence C description Nucleophile => ECO:0000305|PubMed:20304780, ECO:0000305|PubMed:25416785 source Swiss-Prot : SWS_FT_FI1 6) chain H residue 3306 type ACT_SITE sequence C description Nucleophile => ECO:0000305|PubMed:20304780, ECO:0000305|PubMed:25416785 source Swiss-Prot : SWS_FT_FI1 7) chain C residue 1106 type LIPID sequence C description S-palmitoyl cysteine; alternate => ECO:0000269|PubMed:23847046 source Swiss-Prot : SWS_FT_FI10 8) chain D residue 1306 type LIPID sequence C description S-palmitoyl cysteine; alternate => ECO:0000269|PubMed:23847046 source Swiss-Prot : SWS_FT_FI10 9) chain E residue 2106 type LIPID sequence C description S-palmitoyl cysteine; alternate => ECO:0000269|PubMed:23847046 source Swiss-Prot : SWS_FT_FI10 10) chain F residue 2306 type LIPID sequence C description S-palmitoyl cysteine; alternate => ECO:0000269|PubMed:23847046 source Swiss-Prot : SWS_FT_FI10 11) chain G residue 3106 type LIPID sequence C description S-palmitoyl cysteine; alternate => ECO:0000269|PubMed:23847046 source Swiss-Prot : SWS_FT_FI10 12) chain H residue 3306 type LIPID sequence C description S-palmitoyl cysteine; alternate => ECO:0000269|PubMed:23847046 source Swiss-Prot : SWS_FT_FI10 13) chain F residue 2330 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000269|PubMed:15976810 source Swiss-Prot : SWS_FT_FI11 14) chain G residue 3130 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000269|PubMed:15976810 source Swiss-Prot : SWS_FT_FI11 15) chain H residue 3330 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000269|PubMed:15976810 source Swiss-Prot : SWS_FT_FI11 16) chain C residue 1130 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000269|PubMed:15976810 source Swiss-Prot : SWS_FT_FI11 17) chain D residue 1330 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000269|PubMed:15976810 source Swiss-Prot : SWS_FT_FI11 18) chain E residue 2130 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000269|PubMed:15976810 source Swiss-Prot : SWS_FT_FI11 19) chain C residue 1126 type ACT_SITE sequence H description ACT_SITE => ECO:0000305|PubMed:20304780 source Swiss-Prot : SWS_FT_FI2 20) chain D residue 1326 type ACT_SITE sequence H description ACT_SITE => ECO:0000305|PubMed:20304780 source Swiss-Prot : SWS_FT_FI2 21) chain E residue 2126 type ACT_SITE sequence H description ACT_SITE => ECO:0000305|PubMed:20304780 source Swiss-Prot : SWS_FT_FI2 22) chain F residue 2326 type ACT_SITE sequence H description ACT_SITE => ECO:0000305|PubMed:20304780 source Swiss-Prot : SWS_FT_FI2 23) chain G residue 3126 type ACT_SITE sequence H description ACT_SITE => ECO:0000305|PubMed:20304780 source Swiss-Prot : SWS_FT_FI2 24) chain H residue 3326 type ACT_SITE sequence H description ACT_SITE => ECO:0000305|PubMed:20304780 source Swiss-Prot : SWS_FT_FI2 25) chain C residue 1149 type SITE sequence D description Cleavage; by CASP6 => ECO:0000250|UniProtKB:Q99LX0 source Swiss-Prot : SWS_FT_FI3 26) chain D residue 1349 type SITE sequence D description Cleavage; by CASP6 => ECO:0000250|UniProtKB:Q99LX0 source Swiss-Prot : SWS_FT_FI3 27) chain E residue 2149 type SITE sequence D description Cleavage; by CASP6 => ECO:0000250|UniProtKB:Q99LX0 source Swiss-Prot : SWS_FT_FI3 28) chain F residue 2349 type SITE sequence D description Cleavage; by CASP6 => ECO:0000250|UniProtKB:Q99LX0 source Swiss-Prot : SWS_FT_FI3 29) chain G residue 3149 type SITE sequence D description Cleavage; by CASP6 => ECO:0000250|UniProtKB:Q99LX0 source Swiss-Prot : SWS_FT_FI3 30) chain H residue 3349 type SITE sequence D description Cleavage; by CASP6 => ECO:0000250|UniProtKB:Q99LX0 source Swiss-Prot : SWS_FT_FI3 31) chain C residue 1002 type MOD_RES sequence A description N-acetylalanine => ECO:0007744|PubMed:25944712 source Swiss-Prot : SWS_FT_FI4 32) chain D residue 1202 type MOD_RES sequence A description N-acetylalanine => ECO:0007744|PubMed:25944712 source Swiss-Prot : SWS_FT_FI4 33) chain E residue 2002 type MOD_RES sequence A description N-acetylalanine => ECO:0007744|PubMed:25944712 source Swiss-Prot : SWS_FT_FI4 34) chain F residue 2202 type MOD_RES sequence A description N-acetylalanine => ECO:0007744|PubMed:25944712 source Swiss-Prot : SWS_FT_FI4 35) chain G residue 3002 type MOD_RES sequence A description N-acetylalanine => ECO:0007744|PubMed:25944712 source Swiss-Prot : SWS_FT_FI4 36) chain H residue 3202 type MOD_RES sequence A description N-acetylalanine => ECO:0007744|PubMed:25944712 source Swiss-Prot : SWS_FT_FI4 37) chain C residue 1067 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI5 38) chain D residue 1267 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI5 39) chain E residue 2067 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI5 40) chain F residue 2267 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI5 41) chain G residue 3067 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI5 42) chain H residue 3267 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI5 43) chain C residue 1106 type MOD_RES sequence C description Cysteine sulfinic acid (-SO2H); alternate => ECO:0000269|PubMed:12939276 source Swiss-Prot : SWS_FT_FI6 44) chain D residue 1306 type MOD_RES sequence C description Cysteine sulfinic acid (-SO2H); alternate => ECO:0000269|PubMed:12939276 source Swiss-Prot : SWS_FT_FI6 45) chain E residue 2106 type MOD_RES sequence C description Cysteine sulfinic acid (-SO2H); alternate => ECO:0000269|PubMed:12939276 source Swiss-Prot : SWS_FT_FI6 46) chain F residue 2306 type MOD_RES sequence C description Cysteine sulfinic acid (-SO2H); alternate => ECO:0000269|PubMed:12939276 source Swiss-Prot : SWS_FT_FI6 47) chain G residue 3106 type MOD_RES sequence C description Cysteine sulfinic acid (-SO2H); alternate => ECO:0000269|PubMed:12939276 source Swiss-Prot : SWS_FT_FI6 48) chain H residue 3306 type MOD_RES sequence C description Cysteine sulfinic acid (-SO2H); alternate => ECO:0000269|PubMed:12939276 source Swiss-Prot : SWS_FT_FI6 49) chain C residue 1148 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:Q99LX0 source Swiss-Prot : SWS_FT_FI7 50) chain D residue 1348 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:Q99LX0 source Swiss-Prot : SWS_FT_FI7 51) chain E residue 2148 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:Q99LX0 source Swiss-Prot : SWS_FT_FI7 52) chain F residue 2348 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:Q99LX0 source Swiss-Prot : SWS_FT_FI7 53) chain G residue 3148 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:Q99LX0 source Swiss-Prot : SWS_FT_FI7 54) chain H residue 3348 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:Q99LX0 source Swiss-Prot : SWS_FT_FI7 55) chain C residue 1182 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q99LX0 source Swiss-Prot : SWS_FT_FI8 56) chain D residue 1382 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q99LX0 source Swiss-Prot : SWS_FT_FI8 57) chain E residue 2182 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q99LX0 source Swiss-Prot : SWS_FT_FI8 58) chain F residue 2382 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q99LX0 source Swiss-Prot : SWS_FT_FI8 59) chain G residue 3182 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q99LX0 source Swiss-Prot : SWS_FT_FI8 60) chain H residue 3382 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q99LX0 source Swiss-Prot : SWS_FT_FI8 61) chain E residue 2053 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000269|PubMed:23847046 source Swiss-Prot : SWS_FT_FI9 62) chain F residue 2246 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000269|PubMed:23847046 source Swiss-Prot : SWS_FT_FI9 63) chain F residue 2253 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000269|PubMed:23847046 source Swiss-Prot : SWS_FT_FI9 64) chain G residue 3046 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000269|PubMed:23847046 source Swiss-Prot : SWS_FT_FI9 65) chain G residue 3053 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000269|PubMed:23847046 source Swiss-Prot : SWS_FT_FI9 66) chain H residue 3246 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000269|PubMed:23847046 source Swiss-Prot : SWS_FT_FI9 67) chain H residue 3253 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000269|PubMed:23847046 source Swiss-Prot : SWS_FT_FI9 68) chain C residue 1046 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000269|PubMed:23847046 source Swiss-Prot : SWS_FT_FI9 69) chain C residue 1053 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000269|PubMed:23847046 source Swiss-Prot : SWS_FT_FI9 70) chain D residue 1246 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000269|PubMed:23847046 source Swiss-Prot : SWS_FT_FI9 71) chain D residue 1253 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000269|PubMed:23847046 source Swiss-Prot : SWS_FT_FI9 72) chain E residue 2046 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000269|PubMed:23847046 source Swiss-Prot : SWS_FT_FI9

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