eF-site ID 1hju-ABCD PDB Code 1hju Chain A, B, C, D click to enlarge Title Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. Classification HYDROLASE Compound BETA-1,4-GALACTANASE Source (1HJU) Sequence A:  ALTYRGVDWSSVVVEERAGVSYKNTNGNAQPLENILAANG VNTVRQRVWVNPADGNYNLDYNIAIAKRAKAAGLGVYIDF HYSDTWADPAHQTMPAGWPSDIDNLSWKLYNYTLDAANKL QNAGIQPTIVSIGNEIRAGLLWPTGRTENWANIARLLHSA AWGIKDSSLSPKPKIMIHLDNGWDWGTQNWWYTNVLKQGT LELSDFDMMGVSFYPFYSSSATLSALKSSLDNMAKTWNKE IAVVETNWPISCPNPRYSFPSDVKNIPFSPEGQTTFITNV ANIVSSVSRGVGLFYWEPAWIHNANLGSSCADNTMFSQSG QALSSLSVFQRI B:  ALTYRGVDWSSVVVEERAGVSYKNTNGNAQPLENILAANG VNTVRQRVWVNPADGNYNLDYNIAIAKRAKAAGLGVYIDF HYSDTWADPAHQTMPAGWPSDIDNLSWKLYNYTLDAANKL QNAGIQPTIVSIGNEIRAGLLWPTGRTENWANIARLLHSA AWGIKDSSLSPKPKIMIHLDNGWDWGTQNWWYTNVLKQGT LELSDFDMMGVSFYPFYSSSATLSALKSSLDNMAKTWNKE IAVVETNWPISCPNPRYSFPSDVKNIPFSPEGQTTFITNV ANIVSSVSRGVGLFYWEPAWIHNANLGSSCADNTMFSQSG QALSSLSVFQRI C:  ALTYRGVDWSSVVVEERAGVSYKNTNGNAQPLENILAANG VNTVRQRVWVNPADGNYNLDYNIAIAKRAKAAGLGVYIDF HYSDTWADPAHQTMPAGWPSDIDNLSWKLYNYTLDAANKL QNAGIQPTIVSIGNEIRAGLLWPTGRTENWANIARLLHSA AWGIKDSSLSPKPKIMIHLDNGWDWGTQNWWYTNVLKQGT LELSDFDMMGVSFYPFYSSSATLSALKSSLDNMAKTWNKE IAVVETNWPISCPNPRYSFPSDVKNIPFSPEGQTTFITNV ANIVSSVSRGVGLFYWEPAWIHNANLGSSCADNTMFSQSG QALSSLSVFQRI D:  ALTYRGVDWSSVVVEERAGVSYKNTNGNAQPLENILAANG VNTVRQRVWVNPADGNYNLDYNIAIAKRAKAAGLGVYIDF HYSDTWADPAHQTMPAGWPSDIDNLSWKLYNYTLDAANKL QNAGIQPTIVSIGNEIRAGLLWPTGRTENWANIARLLHSA AWGIKDSSLSPKPKIMIHLDNGWDWGTQNWWYTNVLKQGT LELSDFDMMGVSFYPFYSSSATLSALKSSLDNMAKTWNKE IAVVETNWPISCPNPRYSFPSDVKNIPFSPEGQTTFITNV ANIVSSVSRGVGLFYWEPAWIHNANLGSSCADNTMFSQSG QALSSLSVFQRI Description (1)  BETA-1,4-GALACTANASE (E.C.3.2.1.89) Functional site 1) chain A residue 135 type ACT_SITE sequence E description Proton donor => ECO:0000250|UniProtKB:P48841 source Swiss-Prot : SWS_FT_FI1 2) chain B residue 135 type ACT_SITE sequence E description Proton donor => ECO:0000250|UniProtKB:P48841 source Swiss-Prot : SWS_FT_FI1 3) chain C residue 135 type ACT_SITE sequence E description Proton donor => ECO:0000250|UniProtKB:P48841 source Swiss-Prot : SWS_FT_FI1 4) chain D residue 135 type ACT_SITE sequence E description Proton donor => ECO:0000250|UniProtKB:P48841 source Swiss-Prot : SWS_FT_FI1 5) chain A residue 245 type ACT_SITE sequence E description Nucleophile => ECO:0000250|UniProtKB:P48841 source Swiss-Prot : SWS_FT_FI2 6) chain B residue 245 type ACT_SITE sequence E description Nucleophile => ECO:0000250|UniProtKB:P48841 source Swiss-Prot : SWS_FT_FI2 7) chain C residue 245 type ACT_SITE sequence E description Nucleophile => ECO:0000250|UniProtKB:P48841 source Swiss-Prot : SWS_FT_FI2 8) chain D residue 245 type ACT_SITE sequence E description Nucleophile => ECO:0000250|UniProtKB:P48841 source Swiss-Prot : SWS_FT_FI2 9) chain A residue 111 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12761390 source Swiss-Prot : SWS_FT_FI3 10) chain B residue 111 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12761390 source Swiss-Prot : SWS_FT_FI3 11) chain C residue 111 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12761390 source Swiss-Prot : SWS_FT_FI3 12) chain D residue 111 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12761390 source Swiss-Prot : SWS_FT_FI3

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