eF-site ID 1hjx-ABCD PDB Code 1hjx Chain A, B, C, D click to enlarge Title Ligand-induced signalling and conformational change of the 39 kD glycoprotein from human articular chondrocytes Classification SUGAR BINDING PROTEIN Compound CHITINASE-3 LIKE PROTEIN 1 Source ORGANISM_COMMON: HUMAN; ORGANISM_SCIENTIFIC: HOMO SAPIENS; Sequence A:  YKLVCYYTSWSQYREGDGSCFPDALDRFLCTHIIYSFANI SNDHIDTWEWNDVTLYGMLNTLKNRNPNLKTLLSVGGWNF GSQRFSKIASNTQSRRTFIKSVPPFLRTHGFDGLDLAWLY PGRRDKQHFTTLIKEMKAEFIKEAQPGKKQLLLSAALSAG KVTIDSSYDIAKISQHLDFISIMTYDFHGAWRGTTGHHSP LFRGQEDASPDRFSNTDYAVGYMLRLGAPASKLVMGIPTF GRSFTLASSETGVGAPISGPGIPGRFTKEAGTLAYYEICD FLRGATVHRILGQQVPYATKGNQWVGYDDQESVKSKVQYL KDRQLAGAMVWALDLDDFQGSFCGQDLRFPLTNAIKDALA AT B:  YKLVCYYTSWSQYREGDGSCFPDALDRFLCTHIIYSFANI SNDHIDTWEWNDVTLYGMLNTLKNRNPNLKTLLSVGGWNF GSQRFSKIASNTQSRRTFIKSVPPFLRTHGFDGLDLAWLY PGRRDKQHFTTLIKEMKAEFIKEAQPGKKQLLLSAALSAG KVTIDSSYDIAKISQHLDFISIMTYDFHGAWRGTTGHHSP LFRGQEDASPDRFSNTDYAVGYMLRLGAPASKLVMGIPTF GRSFTLASSETGVGAPISGPGIPGRFTKEAGTLAYYEICD FLRGATVHRILGQQVPYATKGNQWVGYDDQESVKSKVQYL KDRQLAGAMVWALDLDDFQGSFCGQDLRFPLTNAIKDALA AT C:  YKLVCYYTSWSQYREGDGSCFPDALDRFLCTHIIYSFANI SNDHIDTWEWNDVTLYGMLNTLKNRNPNLKTLLSVGGWNF GSQRFSKIASNTQSRRTFIKSVPPFLRTHGFDGLDLAWLY PGRRDKQHFTTLIKEMKAEFIKEAKKQLLLSAALSAGKVT IDSSYDIAKISQHLDFISIMTYDFHGAWRGTTGHHSPLFR GQEDASPDRFSNTDYAVGYMLRLGAPASKLVMGIPTFGRS FTLASSETGVGAPISGPGIPGRFTKEAGTLAYYEICDFLR GATVHRILGQQVPYATKGNQWVGYDDQESVKSKVQYLKDR QLAGAMVWALDLDDFQGSFCGQDLRFPLTNAIKDALAAT D:  YKLVCYYTSWSQYREGDGSCFPDALDRFLCTHIIYSFANI SNDHIDTWEWNDVTLYGMLNTLKNRNPNLKTLLSVGGWNF GSQRFSKIASNTQSRRTFIKSVPPFLRTHGFDGLDLAWLY PGRRDKQHFTTLIKEMKAEFIKEAGKKQLLLSAALSAGKV TIDSSYDIAKISQHLDFISIMTYDFHGAWRGTTGHHSPLF RGQEDASPDRFSNTDYAVGYMLRLGAPASKLVMGIPTFGR SFTLASSETGVGAPISGPGIPGRFTKEAGTLAYYEICDFL RGATVHRILGQQVPYATKGNQWVGYDDQESVKSKVQYLKD RQLAGAMVWALDLDDFQGSFCGQDLRFPLTNAIKDALAAT Description Functional site 1) chain A residue 60 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12775711 source Swiss-Prot : SWS_FT_FI3 2) chain B residue 60 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12775711 source Swiss-Prot : SWS_FT_FI3 3) chain C residue 60 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12775711 source Swiss-Prot : SWS_FT_FI3 4) chain D residue 60 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12775711 source Swiss-Prot : SWS_FT_FI3 5) chain A residue 263 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 6) chain B residue 263 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 7) chain C residue 263 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 8) chain D residue 263 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 9) chain A residue 208-233 type prosite sequence FHGAWRGTTGHHSPLFRGQEDASPDR description SUGAR_TRANSPORT_2 Sugar transport proteins signature 2. FhGAWrGTtghhsplFrgQedaspdR source prosite : PS00217 10) chain A residue 70 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU01258 source Swiss-Prot : SWS_FT_FI1 11) chain B residue 352 type BINDING sequence W description BINDING => ECO:0000255|PROSITE-ProRule:PRU01258 source Swiss-Prot : SWS_FT_FI1 12) chain C residue 70 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU01258 source Swiss-Prot : SWS_FT_FI1 13) chain C residue 97 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU01258 source Swiss-Prot : SWS_FT_FI1 14) chain C residue 141 type BINDING sequence Y description BINDING => ECO:0000255|PROSITE-ProRule:PRU01258 source Swiss-Prot : SWS_FT_FI1 15) chain C residue 204 type BINDING sequence M description BINDING => ECO:0000255|PROSITE-ProRule:PRU01258 source Swiss-Prot : SWS_FT_FI1 16) chain C residue 352 type BINDING sequence W description BINDING => ECO:0000255|PROSITE-ProRule:PRU01258 source Swiss-Prot : SWS_FT_FI1 17) chain D residue 70 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU01258 source Swiss-Prot : SWS_FT_FI1 18) chain D residue 97 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU01258 source Swiss-Prot : SWS_FT_FI1 19) chain D residue 141 type BINDING sequence Y description BINDING => ECO:0000255|PROSITE-ProRule:PRU01258 source Swiss-Prot : SWS_FT_FI1 20) chain D residue 204 type BINDING sequence M description BINDING => ECO:0000255|PROSITE-ProRule:PRU01258 source Swiss-Prot : SWS_FT_FI1 21) chain A residue 97 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU01258 source Swiss-Prot : SWS_FT_FI1 22) chain D residue 352 type BINDING sequence W description BINDING => ECO:0000255|PROSITE-ProRule:PRU01258 source Swiss-Prot : SWS_FT_FI1 23) chain A residue 141 type BINDING sequence Y description BINDING => ECO:0000255|PROSITE-ProRule:PRU01258 source Swiss-Prot : SWS_FT_FI1 24) chain A residue 204 type BINDING sequence M description BINDING => ECO:0000255|PROSITE-ProRule:PRU01258 source Swiss-Prot : SWS_FT_FI1 25) chain A residue 352 type BINDING sequence W description BINDING => ECO:0000255|PROSITE-ProRule:PRU01258 source Swiss-Prot : SWS_FT_FI1 26) chain B residue 70 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU01258 source Swiss-Prot : SWS_FT_FI1 27) chain B residue 97 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU01258 source Swiss-Prot : SWS_FT_FI1 28) chain B residue 141 type BINDING sequence Y description BINDING => ECO:0000255|PROSITE-ProRule:PRU01258 source Swiss-Prot : SWS_FT_FI1 29) chain B residue 204 type BINDING sequence M description BINDING => ECO:0000255|PROSITE-ProRule:PRU01258 source Swiss-Prot : SWS_FT_FI1

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