eF-site ID 4s0z-A PDB Code 4s0z Chain A click to enlarge Title Crystal structure of M26V human DJ-1 Classification CHAPERONE Compound Protein DJ-1 Source Homo sapiens (Human) (PARK7_HUMAN) Sequence A:  MASKRALVILAKGAEEMETVIPVDVVRRAGIKVTVAGLAG KDPVQCSRDVVICPDASLEDAKKEGPYDVVVLPGGNLGAQ NLSESAAVKEILKEQENRKGLIAAICAGPTALLAHEIGFG SKVTTHPLAKDKMMNGGHYTYSENRVEKDGLILTSRGPGT SFEFALAIVEALNGKEVAAQVKAPLVLKD Description Functional site 1) chain A residue 29 type sequence A description BINDING SITE FOR RESIDUE EDO A 201 source : AC1 2) chain A residue 131 type sequence D description BINDING SITE FOR RESIDUE EDO A 201 source : AC1 3) chain A residue 173 type sequence N description BINDING SITE FOR RESIDUE EDO A 201 source : AC1 4) chain A residue 177 type sequence V description BINDING SITE FOR RESIDUE EDO A 201 source : AC1 5) chain A residue 179 type sequence A description BINDING SITE FOR RESIDUE EDO A 202 source : AC2 6) chain A residue 182 type sequence K description BINDING SITE FOR RESIDUE EDO A 202 source : AC2 7) chain A residue 76 type sequence N description BINDING SITE FOR RESIDUE EDO A 203 source : AC3 8) chain A residue 107 type sequence A description BINDING SITE FOR RESIDUE EDO A 203 source : AC3 9) chain A residue 128 type sequence L description BINDING SITE FOR RESIDUE EDO A 203 source : AC3 10) chain A residue 15 type sequence E description BINDING SITE FOR RESIDUE EDO A 204 source : AC4 11) chain A residue 28 type sequence R description BINDING SITE FOR RESIDUE EDO A 204 source : AC4 12) chain A residue 126 type sequence H description BINDING SITE FOR RESIDUE EDO A 204 source : AC4 13) chain A residue 158 type sequence P description BINDING SITE FOR RESIDUE EDO A 204 source : AC4 14) chain A residue 184 type sequence P description BINDING SITE FOR RESIDUE EDO A 204 source : AC4 15) chain A residue 76 type sequence N description BINDING SITE FOR RESIDUE ACT A 205 source : AC5 16) chain A residue 107 type sequence A description BINDING SITE FOR RESIDUE ACT A 205 source : AC5 17) chain A residue 132 type sequence K description BINDING SITE FOR RESIDUE ACT A 205 source : AC5 18) chain A residue 106 type LIPID sequence C description S-palmitoyl cysteine; alternate => ECO:0000269|PubMed:23847046 source Swiss-Prot : SWS_FT_FI10 19) chain A residue 149 type SITE sequence D description Cleavage; by CASP6 => ECO:0000250|UniProtKB:Q99LX0 source Swiss-Prot : SWS_FT_FI3 20) chain A residue 106 type ACT_SITE sequence C description Nucleophile => ECO:0000305|PubMed:20304780, ECO:0000305|PubMed:25416785 source Swiss-Prot : SWS_FT_FI1 21) chain A residue 126 type ACT_SITE sequence H description ACT_SITE => ECO:0000305|PubMed:20304780 source Swiss-Prot : SWS_FT_FI2 22) chain A residue 130 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 23) chain A residue 2 type MOD_RES sequence A description N-acetylalanine => ECO:0007744|PubMed:25944712 source Swiss-Prot : SWS_FT_FI4 24) chain A residue 67 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI5 25) chain A residue 106 type MOD_RES sequence C description Cysteine sulfinic acid (-SO2H); alternate => ECO:0000269|PubMed:12939276 source Swiss-Prot : SWS_FT_FI6 26) chain A residue 148 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:Q99LX0 source Swiss-Prot : SWS_FT_FI7 27) chain A residue 182 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q99LX0 source Swiss-Prot : SWS_FT_FI8 28) chain A residue 46 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000269|PubMed:23847046 source Swiss-Prot : SWS_FT_FI9 29) chain A residue 53 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000269|PubMed:23847046 source Swiss-Prot : SWS_FT_FI9

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