eF-site ID 1dys-AB PDB Code 1dys Chain A, B click to enlarge Title Endoglucanase CEL6B from Humicola insolens Classification CELLULASE Compound ENDOGLUCANASE Source (1DYS) Sequence A:  GNPFSGRTLLVNSDYSSKLDQTRQAFLSRGDQTNAAKVKY VQEKVGTFYWISNIFLLRDIDVAIQNARAAKARGENPIVG LVLYNLPDRDCSAGESSGELKLSQNGLNRYKNEYVNPFAQ KLKAASDVQFAVILEPDAIGNMVTGTSAFCRNARGPQQEA IGYAISQLQASHIHLYLDVANGGWLGWADKLEPTAQEVAT ILQKAGNNAKIRGFSSNVSNYNPYSTSNPPPYTSGSPSPD ESRYATNIANAMRQRGLPTQFIIDQSRVALSGARSEWGQW CNVNPAGFGQPFTTNTNNPNVDAIVWVKPGGESDGQCGMG GAPAAGMWFDAYAQMLTQNAHDEIA B:  GNPFSGRTLLVNSDYSSKLDQTRQAFLSRGDQTNAAKVKY VQEKVGTFYWISNIFLLRDIDVAIQNARAAKARGENPIVG LVLYNLPDRDCSAGESSGELKLSQNGLNRYKNEYVNPFAQ KLKAASDVQFAVILEPDAIGNMVTGTSAFCRNARGPQQEA IGYAISQLQASHIHLYLDVANGGWLGWADKLEPTAQEVAT ILQKAGNNAKIRGFSSNVSNYNPYSTSNPPPYTSGSPSPD ESRYATNIANAMRQRGLPTQFIIDQSRVALSGARSEWGQW CNVNPAGFGQPFTTNTNNPNVDAIVWVKPGGESDGQCGMG GAPAAGMWFDAYAQMLTQNAHDEIA Description (1)  ENDOGLUCANASE (E.C.3.2.1.4) Functional site 1) chain A residue 52 type BINDING sequence W description BINDING => ECO:0000250|UniProtKB:Q9C1S9 source Swiss-Prot : SWS_FT_FI3 2) chain B residue 54 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:Q9C1S9 source Swiss-Prot : SWS_FT_FI3 3) chain B residue 183 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q9C1S9 source Swiss-Prot : SWS_FT_FI3 4) chain B residue 186 type BINDING sequence W description BINDING => ECO:0000250|UniProtKB:Q9C1S9 source Swiss-Prot : SWS_FT_FI3 5) chain B residue 222 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q9C1S9 source Swiss-Prot : SWS_FT_FI3 6) chain B residue 282 type BINDING sequence W description BINDING => ECO:0000250|UniProtKB:Q9C1S9 source Swiss-Prot : SWS_FT_FI3 7) chain B residue 310 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:Q9C1S9 source Swiss-Prot : SWS_FT_FI3 8) chain B residue 314 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:Q9C1S9 source Swiss-Prot : SWS_FT_FI3 9) chain A residue 54 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:Q9C1S9 source Swiss-Prot : SWS_FT_FI3 10) chain A residue 183 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q9C1S9 source Swiss-Prot : SWS_FT_FI3 11) chain A residue 186 type BINDING sequence W description BINDING => ECO:0000250|UniProtKB:Q9C1S9 source Swiss-Prot : SWS_FT_FI3 12) chain A residue 222 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q9C1S9 source Swiss-Prot : SWS_FT_FI3 13) chain A residue 282 type BINDING sequence W description BINDING => ECO:0000250|UniProtKB:Q9C1S9 source Swiss-Prot : SWS_FT_FI3 14) chain A residue 310 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:Q9C1S9 source Swiss-Prot : SWS_FT_FI3 15) chain A residue 314 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:Q9C1S9 source Swiss-Prot : SWS_FT_FI3 16) chain B residue 52 type BINDING sequence W description BINDING => ECO:0000250|UniProtKB:Q9C1S9 source Swiss-Prot : SWS_FT_FI3 17) chain A residue 133-142 type prosite sequence AVILEPDAIG description GLYCOSYL_HYDROL_F6_2 Glycosyl hydrolases family 6 signature 2. AVILEPDAIG source prosite : PS00656 18) chain A residue 92 type ACT_SITE sequence D description Proton donor => ECO:0000255|PROSITE-ProRule:PRU10057, ECO:0000303|PubMed:10794732 source Swiss-Prot : SWS_FT_FI1 19) chain B residue 92 type ACT_SITE sequence D description Proton donor => ECO:0000255|PROSITE-ProRule:PRU10057, ECO:0000303|PubMed:10794732 source Swiss-Prot : SWS_FT_FI1 20) chain A residue 139 type ACT_SITE sequence D description Proton donor => ECO:0000255|PROSITE-ProRule:PRU10057, ECO:0000269|PubMed:10794732 source Swiss-Prot : SWS_FT_FI2 21) chain B residue 139 type ACT_SITE sequence D description Proton donor => ECO:0000255|PROSITE-ProRule:PRU10057, ECO:0000269|PubMed:10794732 source Swiss-Prot : SWS_FT_FI2

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