eF-site ID 4ax7-A PDB Code 4ax7 Chain A click to enlarge Title Hypocrea jecorina Cel6A D221A mutant soaked with 4-Methylumbelliferyl- beta-D-cellobioside Classification HYDROLASE Compound EXOGLUCANASE 2 Source (GUX2_HYPJE) Sequence A:  TATYSGNPFVGVTPWANAYYASEVSSLAIPSLTGAMATAA AAVAKVPSFMWLDTLDKTPLMEQTLADIRTANKNGGNYAG QFVVYDLPDRDCAALASNGEYSIADGGVAKYKNYIDTIRQ IVVEYSDIRTLLVIEPASLANLVTNLGTPKCANAQSAYLE CINYAVTQLNLPNVAMYLDAGHAGWLGWPANQDPAAQLFA NVYKNASSPRALRGLATNVANYNGWNITSPPSYTQGNAVY NEKLYIHAIGPLLANHGWSNAFFITDQGRSGKQPTGQQQW GDWCNVIGTGFGIRPSANTGDSLLDSFVWVKPGGECDGTS DSSAPRFDSHCALPDALQPAPQAGAWFQAYFVQLLTNANP SFL Description Functional site 1) chain A residue 169 type catalytic sequence Y description 440 source MCSA : MCSA1 2) chain A residue 174 type catalytic sequence R description 440 source MCSA : MCSA1 3) chain A residue 175 type catalytic sequence D description 440 source MCSA : MCSA1 4) chain A residue 181 type catalytic sequence S description 440 source MCSA : MCSA1 5) chain A residue 221 type catalytic sequence A description 440 source MCSA : MCSA1 6) chain A residue 401 type catalytic sequence D description 440 source MCSA : MCSA1 7) chain A residue 221 type ACT_SITE sequence A description Proton donor => ECO:0000269|PubMed:12188666 source Swiss-Prot : SWS_FT_FI1 8) chain A residue 175 type SITE sequence D description Transition state stabilizer that also modulates the pKa of Asp-245 and may act as a proton acceptor through a water chain => ECO:0000269|PubMed:2377893 source Swiss-Prot : SWS_FT_FI2 9) chain A residue 87 type CARBOHYD sequence T description O-linked (Man...) threonine => ECO:0000269|PubMed:12188666, ECO:0000269|PubMed:8875646 source Swiss-Prot : SWS_FT_FI3 10) chain A residue 97 type CARBOHYD sequence T description O-linked (Man...) threonine => ECO:0000269|PubMed:12188666, ECO:0000269|PubMed:8875646 source Swiss-Prot : SWS_FT_FI3 11) chain A residue 122 type CARBOHYD sequence T description O-linked (Man...) threonine => ECO:0000269|PubMed:12188666, ECO:0000269|PubMed:8875646 source Swiss-Prot : SWS_FT_FI3 12) chain A residue 106 type CARBOHYD sequence S description O-linked (Man...) serine => ECO:0000269|PubMed:12188666, ECO:0000269|PubMed:8875646 source Swiss-Prot : SWS_FT_FI4 13) chain A residue 109 type CARBOHYD sequence S description O-linked (Man...) serine => ECO:0000269|PubMed:12188666, ECO:0000269|PubMed:8875646 source Swiss-Prot : SWS_FT_FI4 14) chain A residue 110 type CARBOHYD sequence S description O-linked (Man...) serine => ECO:0000269|PubMed:12188666, ECO:0000269|PubMed:8875646 source Swiss-Prot : SWS_FT_FI4 15) chain A residue 115 type CARBOHYD sequence S description O-linked (Man...) serine => ECO:0000269|PubMed:12188666, ECO:0000269|PubMed:8875646 source Swiss-Prot : SWS_FT_FI4 16) chain A residue 289 type CARBOHYD sequence N description N-linked (GlcNAc) asparagine => ECO:0000269|PubMed:12188666, ECO:0000269|PubMed:8875646 source Swiss-Prot : SWS_FT_FI5 17) chain A residue 310 type CARBOHYD sequence N description N-linked (GlcNAc...) (high mannose) asparagine => ECO:0000269|PubMed:12188666, ECO:0000269|PubMed:8875646 source Swiss-Prot : SWS_FT_FI6 18) chain A residue 167-183 type prosite sequence VVYDLPDRDCAALASNG description GLYCOSYL_HYDROL_F6_1 Glycosyl hydrolases family 6 signature 1. VvYdlPdRDCAalASnG source prosite : PS00655

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