eF-site ID 4hko-A PDB Code 4hko Chain A click to enlarge Title Crystal Structures of Mutant Endo-beta-1,4-xylanase II (E177Q) in the apo form Classification HYDROLASE Compound Endo-1,4-beta-xylanase 2 Source Hypocrea jecorina (strain ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30) (Trichoderma reesei) (XYN2_HYPJE) Sequence A:  TIQPGTGYNNGYFYSYWNDGHGGVTYTNGPGGQFSVNWSN SGNFVGGKGWQPGTKNKVINFSGSYNPNGNSYLSVYGWSR NPLIEYYIVENFGTYNPSTGATKLGEVTSDGSVYDIYRTQ RVNQPSIIGTATFYQYWSVRRNHRSSGSVNTANHFNAWAQ QGLTLGTMDYQIVAVQGYFSSGSASITVS Description Functional site 1) chain A residue 82 type sequence N description BINDING SITE FOR RESIDUE IOD A 500 source : AC1 2) chain A residue 146 type sequence S description BINDING SITE FOR RESIDUE IOD A 500 source : AC1 3) chain A residue 2 type sequence T description BINDING SITE FOR RESIDUE IOD A 502 source : AC2 4) chain A residue 169 type sequence M description BINDING SITE FOR RESIDUE IOD A 502 source : AC2 5) chain A residue 68 type sequence P description BINDING SITE FOR RESIDUE IOD A 503 source : AC3 6) chain A residue 70 type sequence G description BINDING SITE FOR RESIDUE IOD A 503 source : AC3 7) chain A residue 123 type sequence V description BINDING SITE FOR RESIDUE IOD A 504 source : AC4 8) chain A residue 125 type sequence Q description BINDING SITE FOR RESIDUE IOD A 504 source : AC4 9) chain A residue 131 type sequence T description BINDING SITE FOR RESIDUE IOD A 505 source : AC5 10) chain A residue 83-93 type prosite sequence PLIEYYIVENF description GH11_1 Glycosyl hydrolases family 11 (GH11) active site signature 1. PLiEYYIVEnF source prosite : PS00776 11) chain A residue 87 type ACT_SITE sequence Y description Nucleophile => ECO:0000269|PubMed:26392527, ECO:0000305|PubMed:24419374 source Swiss-Prot : SWS_FT_FI1 12) chain A residue 178 type ACT_SITE sequence G description Proton donor => ECO:0000269|PubMed:26392527, ECO:0000305|PubMed:24419374 source Swiss-Prot : SWS_FT_FI2 13) chain A residue 74 type BINDING sequence L description BINDING => ECO:0000269|PubMed:24419374 source Swiss-Prot : SWS_FT_FI3 14) chain A residue 78 type BINDING sequence G description BINDING => ECO:0000269|PubMed:24419374 source Swiss-Prot : SWS_FT_FI3 15) chain A residue 89 type BINDING sequence I description BINDING => ECO:0000269|PubMed:24419374 source Swiss-Prot : SWS_FT_FI3 16) chain A residue 123 type BINDING sequence V description BINDING => ECO:0000269|PubMed:24419374 source Swiss-Prot : SWS_FT_FI3 17) chain A residue 127 type BINDING sequence S description BINDING => ECO:0000269|PubMed:24419374 source Swiss-Prot : SWS_FT_FI3 18) chain A residue 137 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:24419374 source Swiss-Prot : SWS_FT_FI3 19) chain A residue 172 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:24419374 source Swiss-Prot : SWS_FT_FI3 20) chain A residue 2 type MOD_RES sequence T description Pyrrolidone carboxylic acid => ECO:0000269|PubMed:1369024, ECO:0000269|PubMed:16790934 source Swiss-Prot : SWS_FT_FI4 21) chain A residue 39 type CARBOHYD sequence W description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI5 22) chain A residue 62 type CARBOHYD sequence F description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI5

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