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 1067 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI5 2) chain D residue 1267 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI5 3) chain E residue 2067 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI5 4) chain F residue 2267 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI5 5) chain G residue 3067 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI5 6) chain H residue 3267 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI5 7) 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 8) 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 9) 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 10) 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 11) 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 12) 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 13) chain C residue 1148 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:Q99LX0 source Swiss-Prot : SWS_FT_FI7 14) chain D residue 1348 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:Q99LX0 source Swiss-Prot : SWS_FT_FI7 15) chain E residue 2148 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:Q99LX0 source Swiss-Prot : SWS_FT_FI7 16) chain F residue 2348 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:Q99LX0 source Swiss-Prot : SWS_FT_FI7 17) chain G residue 3148 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:Q99LX0 source Swiss-Prot : SWS_FT_FI7 18) chain H residue 3348 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:Q99LX0 source Swiss-Prot : SWS_FT_FI7 19) 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 20) 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 21) 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 22) 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 23) 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 24) 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 25) chain C residue 1126 type ACT_SITE sequence H description ACT_SITE => ECO:0000305|PubMed:20304780 source Swiss-Prot : SWS_FT_FI2 26) chain D residue 1326 type ACT_SITE sequence H description ACT_SITE => ECO:0000305|PubMed:20304780 source Swiss-Prot : SWS_FT_FI2 27) chain E residue 2126 type ACT_SITE sequence H description ACT_SITE => ECO:0000305|PubMed:20304780 source Swiss-Prot : SWS_FT_FI2 28) chain F residue 2326 type ACT_SITE sequence H description ACT_SITE => ECO:0000305|PubMed:20304780 source Swiss-Prot : SWS_FT_FI2 29) chain G residue 3126 type ACT_SITE sequence H description ACT_SITE => ECO:0000305|PubMed:20304780 source Swiss-Prot : SWS_FT_FI2 30) chain H residue 3326 type ACT_SITE sequence H description ACT_SITE => ECO:0000305|PubMed:20304780 source Swiss-Prot : SWS_FT_FI2 31) chain C residue 1149 type SITE sequence D description Cleavage; by CASP6 => ECO:0000250|UniProtKB:Q99LX0 source Swiss-Prot : SWS_FT_FI3 32) chain D residue 1349 type SITE sequence D description Cleavage; by CASP6 => ECO:0000250|UniProtKB:Q99LX0 source Swiss-Prot : SWS_FT_FI3 33) chain E residue 2149 type SITE sequence D description Cleavage; by CASP6 => ECO:0000250|UniProtKB:Q99LX0 source Swiss-Prot : SWS_FT_FI3 34) chain F residue 2349 type SITE sequence D description Cleavage; by CASP6 => ECO:0000250|UniProtKB:Q99LX0 source Swiss-Prot : SWS_FT_FI3 35) chain G residue 3149 type SITE sequence D description Cleavage; by CASP6 => ECO:0000250|UniProtKB:Q99LX0 source Swiss-Prot : SWS_FT_FI3 36) chain H residue 3349 type SITE sequence D description Cleavage; by CASP6 => ECO:0000250|UniProtKB:Q99LX0 source Swiss-Prot : SWS_FT_FI3 37) chain C residue 1002 type MOD_RES sequence A description N-acetylalanine => ECO:0007744|PubMed:25944712 source Swiss-Prot : SWS_FT_FI4 38) chain D residue 1202 type MOD_RES sequence A description N-acetylalanine => ECO:0007744|PubMed:25944712 source Swiss-Prot : SWS_FT_FI4 39) chain E residue 2002 type MOD_RES sequence A description N-acetylalanine => ECO:0007744|PubMed:25944712 source Swiss-Prot : SWS_FT_FI4 40) chain F residue 2202 type MOD_RES sequence A description N-acetylalanine => ECO:0007744|PubMed:25944712 source Swiss-Prot : SWS_FT_FI4 41) chain G residue 3002 type MOD_RES sequence A description N-acetylalanine => ECO:0007744|PubMed:25944712 source Swiss-Prot : SWS_FT_FI4 42) chain H residue 3202 type MOD_RES sequence A description N-acetylalanine => ECO:0007744|PubMed:25944712 source Swiss-Prot : SWS_FT_FI4 43) 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 44) 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 45) 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 46) 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 47) 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 48) 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 49) chain C residue 1182 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q99LX0 source Swiss-Prot : SWS_FT_FI8 50) chain D residue 1382 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q99LX0 source Swiss-Prot : SWS_FT_FI8 51) chain E residue 2182 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q99LX0 source Swiss-Prot : SWS_FT_FI8 52) chain F residue 2382 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q99LX0 source Swiss-Prot : SWS_FT_FI8 53) chain G residue 3182 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q99LX0 source Swiss-Prot : SWS_FT_FI8 54) chain H residue 3382 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q99LX0 source Swiss-Prot : SWS_FT_FI8 55) chain E residue 2053 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000269|PubMed:23847046 source Swiss-Prot : SWS_FT_FI9 56) chain F residue 2246 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000269|PubMed:23847046 source Swiss-Prot : SWS_FT_FI9 57) chain F residue 2253 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000269|PubMed:23847046 source Swiss-Prot : SWS_FT_FI9 58) chain G residue 3046 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000269|PubMed:23847046 source Swiss-Prot : SWS_FT_FI9 59) chain G residue 3053 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000269|PubMed:23847046 source Swiss-Prot : SWS_FT_FI9 60) chain H residue 3246 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000269|PubMed:23847046 source Swiss-Prot : SWS_FT_FI9 61) chain H residue 3253 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000269|PubMed:23847046 source Swiss-Prot : SWS_FT_FI9 62) chain C residue 1046 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000269|PubMed:23847046 source Swiss-Prot : SWS_FT_FI9 63) chain C residue 1053 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000269|PubMed:23847046 source Swiss-Prot : SWS_FT_FI9 64) chain D residue 1246 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000269|PubMed:23847046 source Swiss-Prot : SWS_FT_FI9 65) chain D residue 1253 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000269|PubMed:23847046 source Swiss-Prot : SWS_FT_FI9 66) chain E residue 2046 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000269|PubMed:23847046 source Swiss-Prot : SWS_FT_FI9 67) chain C residue 1106 type LIPID sequence C description S-palmitoyl cysteine; alternate => ECO:0000269|PubMed:23847046 source Swiss-Prot : SWS_FT_FI10 68) chain D residue 1306 type LIPID sequence C description S-palmitoyl cysteine; alternate => ECO:0000269|PubMed:23847046 source Swiss-Prot : SWS_FT_FI10 69) chain E residue 2106 type LIPID sequence C description S-palmitoyl cysteine; alternate => ECO:0000269|PubMed:23847046 source Swiss-Prot : SWS_FT_FI10 70) chain F residue 2306 type LIPID sequence C description S-palmitoyl cysteine; alternate => ECO:0000269|PubMed:23847046 source Swiss-Prot : SWS_FT_FI10 71) chain G residue 3106 type LIPID sequence C description S-palmitoyl cysteine; alternate => ECO:0000269|PubMed:23847046 source Swiss-Prot : SWS_FT_FI10 72) chain H residue 3306 type LIPID sequence C description S-palmitoyl cysteine; alternate => ECO:0000269|PubMed:23847046 source Swiss-Prot : SWS_FT_FI10

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