eF-site ID 2axe-A PDB Code 2axe Chain A click to enlarge Title IODINATED COMPLEX OF ACETYL XYLAN ESTERASE AT 1.80 ANGSTROMS Classification HYDROLASE Compound ACETYL XYLAN ESTERASE Source ORGANISM_SCIENTIFIC: Penicillium purpurogenum; Sequence A:  SCPAIHVFGARETTASPGYGSSSTVVNGVLSAXPGSTAEA INYPACGGQSSCGGASYSSSVAQGIAAVASAVNSFNSQCP STKIVLVGYSQGGEIMDVALCGGGDPNQGYTNTAVQLSSS AVNMVKAAIFMGDPMFRAGLSYEVGTCAAGGFDQRPAGFS CPSAAKIKSYCDASDPXCCNGSNAATHQGYGSEYGSQALA FVKSKLG Description Functional site 1) chain A residue 90 type sequence S description THESE RESIDUES FORM THE CATALYTIC TRIAD. source : CAT 2) chain A residue 175 type sequence D description THESE RESIDUES FORM THE CATALYTIC TRIAD. source : CAT 3) chain A residue 187 type sequence H description THESE RESIDUES FORM THE CATALYTIC TRIAD. source : CAT 4) chain A residue 146 type sequence T description BINDING SITE FOR RESIDUE SO4 A 209 source : AC1 5) chain A residue 172 type sequence D description BINDING SITE FOR RESIDUE SO4 A 209 source : AC1 6) chain A residue 173 type sequence A description BINDING SITE FOR RESIDUE SO4 A 209 source : AC1 7) chain A residue 174 type sequence S description BINDING SITE FOR RESIDUE SO4 A 209 source : AC1 8) chain A residue 180 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI2 9) chain A residue 13 type catalytic sequence T description 431 source MCSA : MCSA1 10) chain A residue 90 type catalytic sequence S description 431 source MCSA : MCSA1 11) chain A residue 91 type catalytic sequence Q description 431 source MCSA : MCSA1 12) chain A residue 175 type catalytic sequence D description 431 source MCSA : MCSA1 13) chain A residue 187 type catalytic sequence H description 431 source MCSA : MCSA1 14) chain A residue 90 type ACT_SITE sequence S description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 15) chain A residue 175 type ACT_SITE sequence D description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 16) chain A residue 187 type ACT_SITE sequence H description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 17) chain A residue 84-93 type prosite sequence IVLVGYSQGG description LIPASE_SER Lipases, serine active site. IVLVGYSQGG source prosite : PS00120

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