eF-site ID 5nr8-A PDB Code 5nr8 Chain A click to enlarge Title Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound 7a Classification HYDROLASE Compound Chitotriosidase-1 Source (CHIT1_HUMAN) Sequence A:  AKLVCYFTNWAQYRQGEARFLPKDLDPSLCTHLIYAFAGM TNHQLSTTEWNDETLYQEFNGLKKMNPKLKTLLAIGGWNF GTQKFTDMVATANNRQTFVNSAIRFLRKYSFDGLDLDWEY PGSQGSPAVDKERFTTLVQDLANAFQQEAQTSGKERLLLS AAVPAGQTYVDAGYEVDKIAQNLDFVNLMAYDFHGSWEKV TGHNSPLYKRQEESGAAASLNVDAAVQQWLQKGTPASKLI LGMPTYGRSFTLASSSDTRVGAPATGSGTPGPFTKEGGML AYYEVCSWKGATKQRIQDQKVPYIFRDNQWVGFDDVESFK TKVSYLKQKGLGGAMVWALDLDDFAGFSCNQGRYPLIQTL RQELSLVPRGSHHHHHH Description (1)  Chitotriosidase-1 (E.C.3.2.1.14) Functional site 1) chain A residue 27 type sequence Y description binding site for residue 95N A 401 source : AC1 2) chain A residue 99 type sequence W description binding site for residue 95N A 401 source : AC1 3) chain A residue 138 type sequence D description binding site for residue 95N A 401 source : AC1 4) chain A residue 140 type sequence E description binding site for residue 95N A 401 source : AC1 5) chain A residue 183 type sequence A description binding site for residue 95N A 401 source : AC1 6) chain A residue 210 type sequence M description binding site for residue 95N A 401 source : AC1 7) chain A residue 212 type sequence Y description binding site for residue 95N A 401 source : AC1 8) chain A residue 213 type sequence D description binding site for residue 95N A 401 source : AC1 9) chain A residue 267 type sequence Y description binding site for residue 95N A 401 source : AC1 10) chain A residue 295 type sequence T description binding site for residue 95N A 401 source : AC1 11) chain A residue 297 type sequence E description binding site for residue 95N A 401 source : AC1 12) chain A residue 300 type sequence M description binding site for residue 95N A 401 source : AC1 13) chain A residue 356 type sequence M description binding site for residue 95N A 401 source : AC1 14) chain A residue 358 type sequence W description binding site for residue 95N A 401 source : AC1 15) chain A residue 362 type sequence L description binding site for residue 95N A 401 source : AC1 16) chain A residue 99 type sequence W description binding site for residue GOL A 402 source : AC2 17) chain A residue 269 type sequence R description binding site for residue GOL A 402 source : AC2 18) chain A residue 300 type sequence M description binding site for residue GOL A 402 source : AC2 19) chain A residue 390 type sequence R description binding site for residue GOL A 402 source : AC2 20) chain A residue 391 type sequence G description binding site for residue GOL A 402 source : AC2 21) chain A residue 202 type sequence Q description binding site for residue GOL A 403 source : AC3 22) chain A residue 204 type sequence L description binding site for residue GOL A 403 source : AC3 23) chain A residue 205 type sequence D description binding site for residue GOL A 403 source : AC3 24) chain A residue 259 type sequence K description binding site for residue GOL A 403 source : AC3 25) chain A residue 49 type sequence S description binding site for residue GOL A 404 source : AC4 26) chain A residue 51 type sequence C description binding site for residue GOL A 404 source : AC4 27) chain A residue 52 type sequence T description binding site for residue GOL A 404 source : AC4 28) chain A residue 87 type sequence N description binding site for residue GOL A 404 source : AC4 29) chain A residue 387 type sequence L description binding site for residue GOL A 404 source : AC4 30) chain A residue 389 type sequence P description binding site for residue GOL A 404 source : AC4 31) chain A residue 30 type sequence N description binding site for residue GOL A 405 source : AC5 32) chain A residue 58 type sequence F description binding site for residue GOL A 405 source : AC5 33) chain A residue 69 type sequence T description binding site for residue GOL A 405 source : AC5 34) chain A residue 70 type sequence E description binding site for residue GOL A 405 source : AC5 35) chain A residue 31 type sequence W description binding site for residue GOL A 406 source : AC6 36) chain A residue 35 type sequence R description binding site for residue GOL A 406 source : AC6 37) chain A residue 295 type sequence T description binding site for residue GOL A 406 source : AC6 38) chain A residue 297 type sequence E description binding site for residue GOL A 406 source : AC6 39) chain A residue 141 type sequence Y description binding site for residue GOL A 407 source : AC7 40) chain A residue 185 type sequence P description binding site for residue GOL A 407 source : AC7 41) chain A residue 186 type sequence A description binding site for residue GOL A 407 source : AC7 42) chain A residue 210 type sequence M description binding site for residue GOL A 407 source : AC7 43) chain A residue 212 type sequence Y description binding site for residue GOL A 407 source : AC7 44) chain A residue 213 type sequence D description binding site for residue GOL A 407 source : AC7 45) chain A residue 214 type sequence F description binding site for residue GOL A 407 source : AC7 46) chain A residue 132-140 type prosite sequence FDGLDLDWE description GH18_1 Glycosyl hydrolases family 18 (GH18) active site signature. FDGLDLDwE source prosite : PS01095 47) chain A residue 140 type ACT_SITE sequence E description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01258 source Swiss-Prot : SWS_FT_FI1 48) chain A residue 70 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU01258 source Swiss-Prot : SWS_FT_FI2 49) chain A residue 97 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU01258 source Swiss-Prot : SWS_FT_FI2 50) chain A residue 141 type BINDING sequence Y description BINDING => ECO:0000255|PROSITE-ProRule:PRU01258 source Swiss-Prot : SWS_FT_FI2 51) chain A residue 210 type BINDING sequence M description BINDING => ECO:0000255|PROSITE-ProRule:PRU01258 source Swiss-Prot : SWS_FT_FI2 52) chain A residue 358 type BINDING sequence W description BINDING => ECO:0000255|PROSITE-ProRule:PRU01258 source Swiss-Prot : SWS_FT_FI2 53) chain A residue 100 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine; in variant S-102 => ECO:0000269|PubMed:19725875 source Swiss-Prot : SWS_FT_FI3

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