eF-site ID 1pp4-AB PDB Code 1pp4 Chain A, B click to enlarge Title The crystal structure of rhamnogalacturonan acetylesterase in space group P3121 Classification HYDROLASE Compound Rhamnogalacturonan acetylesterase Source Aspergillus aculeatus (RHA1_ASPAC) Sequence A:  TTVYLAGDSTMAKNGGGSGTNGWGEYLASYLSATVVNDAV AGRSARSYTREGRFENIADVVTAGDYVIVEFGHNDGGSLS TDNGRTDCSGTGAEVCYSVYDGVNETILTFPAYLENAAKL FTAKGAKVILSSQTPNNPWETGTFVNSPTRFVEYAELAAE VAGVEYVDHWSYVDSIYETLGNATVNSYFPIDHTHTSPAG AEVVAEAFLKAVVCTGTSLKSVLTTTSFEGTCL B:  TTVYLAGDSTMAKNGGGSGTNGWGEYLASYLSATVVNDAV AGRSARSYTREGRFENIADVVTAGDYVIVEFGHNDGGSLS TDNGRTDCSGTGAEVCYSVYDGVNETILTFPAYLENAAKL FTAKGAKVILSSQTPNNPWETGTFVNSPTRFVEYAELAAE VAGVEYVDHWSYVDSIYETLGNATVNSYFPIDHTHTSPAG AEVVAEAFLKAVVCTGTSLKSVLTTTSFEGTCL Description Functional site 1) chain A residue 9 type catalytic sequence S description 705 source MCSA : MCSA1 2) chain A residue 42 type catalytic sequence G description 705 source MCSA : MCSA1 3) chain A residue 74 type catalytic sequence N description 705 source MCSA : MCSA1 4) chain A residue 192 type catalytic sequence D description 705 source MCSA : MCSA1 5) chain A residue 195 type catalytic sequence H description 705 source MCSA : MCSA1 6) chain B residue 9 type catalytic sequence S description 705 source MCSA : MCSA2 7) chain B residue 42 type catalytic sequence G description 705 source MCSA : MCSA2 8) chain B residue 74 type catalytic sequence N description 705 source MCSA : MCSA2 9) chain B residue 192 type catalytic sequence D description 705 source MCSA : MCSA2 10) chain B residue 195 type catalytic sequence H description 705 source MCSA : MCSA2 11) chain A residue 9 type ACT_SITE sequence S description Nucleophile => ECO:0000305|PubMed:10801485 source Swiss-Prot : SWS_FT_FI1 12) chain B residue 9 type ACT_SITE sequence S description Nucleophile => ECO:0000305|PubMed:10801485 source Swiss-Prot : SWS_FT_FI1 13) chain A residue 192 type ACT_SITE sequence D description ACT_SITE => ECO:0000269|PubMed:10801485 source Swiss-Prot : SWS_FT_FI2 14) chain A residue 195 type ACT_SITE sequence H description ACT_SITE => ECO:0000269|PubMed:10801485 source Swiss-Prot : SWS_FT_FI2 15) chain B residue 192 type ACT_SITE sequence D description ACT_SITE => ECO:0000269|PubMed:10801485 source Swiss-Prot : SWS_FT_FI2 16) chain B residue 195 type ACT_SITE sequence H description ACT_SITE => ECO:0000269|PubMed:10801485 source Swiss-Prot : SWS_FT_FI2 17) chain A residue 104 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10801485, ECO:0000269|PubMed:11752785, ECO:0000269|PubMed:18645234 source Swiss-Prot : SWS_FT_FI3 18) chain B residue 104 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10801485, ECO:0000269|PubMed:11752785, ECO:0000269|PubMed:18645234 source Swiss-Prot : SWS_FT_FI3 19) chain A residue 182 type CARBOHYD sequence N description N-linked (GlcNAc...) (high mannose) asparagine => ECO:0000269|PubMed:10801485, ECO:0000269|PubMed:11752785, ECO:0000269|PubMed:18645234 source Swiss-Prot : SWS_FT_FI4 20) chain B residue 182 type CARBOHYD sequence N description N-linked (GlcNAc...) (high mannose) asparagine => ECO:0000269|PubMed:10801485, ECO:0000269|PubMed:11752785, ECO:0000269|PubMed:18645234 source Swiss-Prot : SWS_FT_FI4

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