eF-site ID 4xqd-AB PDB Code 4xqd Chain A, B click to enlarge Title X-ray structure analysis of xylanase-WT at pH4.0 Classification HYDROLASE Compound Endo-1,4-beta-xylanase 2 Source (XYN2_HYPJE) Sequence A:  IQPGTGYNNGYFYSYWNDGHGGVTYTNGPGGQFSVNWSNS GNFVGGKGWQPGTKNKVINFSGSYNPNGNSYLSVYGWSRN PLIEYYIVENFGTYNPSTGATKLGEVTSDGSVYDIYRTQR VNQPSIIGTATFYQYWSVRRNHRSSGSVNTANHFNAWAQQ GLTLGTMDYQIVAVEGYFSSGSASITVS B:  TIQPGTGYNNGYFYSYWNDGHGGVTYTNGPGGQFSVNWSN SGNFVGGKGWQPGTKNKVINFSGSYNPNGNSYLSVYGWSR 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 184 type sequence S description binding site for residue IOD A 202 source : AC2 4) chain A residue 123 type sequence V description binding site for residue IOD A 203 source : AC3 5) chain A residue 82 type sequence N description binding site for residue TRS A 204 source : AC4 6) chain A residue 92 type sequence N description binding site for residue TRS A 204 source : AC4 7) chain A residue 145 type sequence R description binding site for residue TRS A 204 source : AC4 8) chain A residue 146 type sequence S description binding site for residue TRS A 204 source : AC4 9) chain B residue 82 type sequence N description binding site for residue IOD B 201 source : AC5 10) chain B residue 146 type sequence S description binding site for residue IOD B 201 source : AC5 11) chain B residue 184 type sequence S description binding site for residue IOD B 202 source : AC6 12) chain B residue 24 type sequence G description binding site for residue IOD B 203 source : AC7 13) chain B residue 26 type sequence T description binding site for residue IOD B 203 source : AC7 14) chain B residue 38 type sequence N description binding site for residue IOD B 203 source : AC7 15) 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 16) chain B residue 87 type ACT_SITE sequence Y description Nucleophile => ECO:0000269|PubMed:26392527, ECO:0000305|PubMed:24419374 source Swiss-Prot : SWS_FT_FI1 17) chain B 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 18) chain A residue 39 type CARBOHYD sequence W description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI5 19) chain A residue 62 type CARBOHYD sequence F description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI5 20) chain B residue 39 type CARBOHYD sequence W description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI5 21) chain B residue 62 type CARBOHYD sequence F description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI5 22) 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 23) chain B residue 178 type ACT_SITE sequence G description Proton donor => ECO:0000269|PubMed:26392527, ECO:0000305|PubMed:24419374 source Swiss-Prot : SWS_FT_FI2 24) chain A residue 74 type BINDING sequence L description BINDING => ECO:0000269|PubMed:24419374 source Swiss-Prot : SWS_FT_FI3 25) chain B residue 89 type BINDING sequence I description BINDING => ECO:0000269|PubMed:24419374 source Swiss-Prot : SWS_FT_FI3 26) chain B residue 123 type BINDING sequence V description BINDING => ECO:0000269|PubMed:24419374 source Swiss-Prot : SWS_FT_FI3 27) chain B residue 127 type BINDING sequence S description BINDING => ECO:0000269|PubMed:24419374 source Swiss-Prot : SWS_FT_FI3 28) chain B residue 137 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:24419374 source Swiss-Prot : SWS_FT_FI3 29) chain B residue 172 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:24419374 source Swiss-Prot : SWS_FT_FI3 30) chain A residue 78 type BINDING sequence G description BINDING => ECO:0000269|PubMed:24419374 source Swiss-Prot : SWS_FT_FI3 31) chain A residue 89 type BINDING sequence I description BINDING => ECO:0000269|PubMed:24419374 source Swiss-Prot : SWS_FT_FI3 32) chain A residue 123 type BINDING sequence V description BINDING => ECO:0000269|PubMed:24419374 source Swiss-Prot : SWS_FT_FI3 33) chain A residue 127 type BINDING sequence S description BINDING => ECO:0000269|PubMed:24419374 source Swiss-Prot : SWS_FT_FI3 34) chain A residue 137 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:24419374 source Swiss-Prot : SWS_FT_FI3 35) chain A residue 172 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:24419374 source Swiss-Prot : SWS_FT_FI3 36) chain B residue 74 type BINDING sequence L description BINDING => ECO:0000269|PubMed:24419374 source Swiss-Prot : SWS_FT_FI3 37) chain B residue 78 type BINDING sequence G description BINDING => ECO:0000269|PubMed:24419374 source Swiss-Prot : SWS_FT_FI3 38) 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 39) 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

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