eF-site ID 4xqw-A PDB Code 4xqw Chain A click to enlarge Title X-ray structure analysis of xylanase-N44E with MES at pH6.0 Classification HYDROLASE Compound Endo-1,4-beta-xylanase 2 Source (XYN2_HYPJE) Sequence A:  TIQPGTGYNNGYFYSYWNDGHGGVTYTNGPGGQFSVNWSN SGEFVGGKGWQPGTKNKVINFSGSYNPNGNSYLSVYGWSR NPLIEYYIVENFGTYNPSTGATKLGEVTSDGSVYDIYRTQ RVNQPSIIGTATFYQYWSVRRNHRSSGSVNTANHFNAWAQ QGLTLGTMDYQIVAVEGYFSSGSASITVS Description Functional site 1) chain A residue 82 type sequence N description binding site for residue IOD A 201 source : AC1 2) chain A residue 146 type sequence S description binding site for residue IOD A 201 source : AC1 3) chain A residue 2 type sequence T description binding site for residue IOD A 203 source : AC2 4) chain A residue 169 type sequence M description binding site for residue IOD A 203 source : AC2 5) chain A residue 123 type sequence V description binding site for residue IOD A 204 source : AC3 6) chain A residue 125 type sequence Q description binding site for residue IOD A 204 source : AC3 7) chain A residue 68 type sequence P description binding site for residue IOD A 205 source : AC4 8) chain A residue 70 type sequence G description binding site for residue IOD A 205 source : AC4 9) chain A residue 44 type sequence E description binding site for residue MES A 206 source : AC5 10) chain A residue 46 type sequence V description binding site for residue MES A 206 source : AC5 11) chain A residue 73 type sequence Y description binding site for residue MES A 206 source : AC5 12) chain A residue 77 type sequence Y description binding site for residue MES A 206 source : AC5 13) chain A residue 86 type sequence E description binding site for residue MES A 206 source : AC5 14) chain A residue 88 type sequence Y description binding site for residue MES A 206 source : AC5 15) chain A residue 122 type sequence R description binding site for residue MES A 206 source : AC5 16) chain A residue 136 type sequence Q description binding site for residue MES A 206 source : AC5 17) chain A residue 138 type sequence W description binding site for residue MES A 206 source : AC5 18) chain A residue 177 type sequence E description binding site for residue MES A 206 source : AC5 19) chain A residue 74 type BINDING sequence L description BINDING => ECO:0000269|PubMed:24419374 source Swiss-Prot : SWS_FT_FI3 20) chain A residue 78 type BINDING sequence G description BINDING => ECO:0000269|PubMed:24419374 source Swiss-Prot : SWS_FT_FI3 21) chain A residue 89 type BINDING sequence I description BINDING => ECO:0000269|PubMed:24419374 source Swiss-Prot : SWS_FT_FI3 22) chain A residue 123 type BINDING sequence V description BINDING => ECO:0000269|PubMed:24419374 source Swiss-Prot : SWS_FT_FI3 23) chain A residue 127 type BINDING sequence S description BINDING => ECO:0000269|PubMed:24419374 source Swiss-Prot : SWS_FT_FI3 24) chain A residue 137 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:24419374 source Swiss-Prot : SWS_FT_FI3 25) chain A residue 172 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:24419374 source Swiss-Prot : SWS_FT_FI3 26) 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 27) chain A residue 39 type CARBOHYD sequence W description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI5 28) chain A residue 62 type CARBOHYD sequence F description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI5 29) 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 30) chain A residue 174-185 type prosite sequence VAVEGYFSSGSA description GH11_2 Glycosyl hydrolases family 11 (GH11) active site signature 2. VavEGYFSSGsA source prosite : PS00777 31) 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 32) 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

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