eF-site ID 1isp-A PDB Code 1isp Chain A click to enlarge Title Crystal structure of Bacillus subtilis lipase at 1.3A resolution Classification HYDROLASE Compound lipase Source Bacillus subtilis (LIP_BACSU) Sequence A:  EHNPVVMVHGIGGASFNFAGIKSYLVSQGWSRDKLYAVDF WDKTGTNYNNGPVLSRFVQKVLDETGAKKVDIVAHSMGGA NTLYYIKNLDGGNKVANVVTLGGANRLTTGKALPGTDPNQ KILYTSIYSSADMIVMNYLSRLDGARNVQIHGVGHIGLLY SSQVNSLIKEGLNGGGQNT Description Functional site 1) chain A residue 11 type sequence G description BINDING SITE FOR RESIDUE GOL A 200 source : AC1 2) chain A residue 12 type sequence I description BINDING SITE FOR RESIDUE GOL A 200 source : AC1 3) chain A residue 14 type sequence G description BINDING SITE FOR RESIDUE GOL A 200 source : AC1 4) chain A residue 18 type sequence N description BINDING SITE FOR RESIDUE GOL A 200 source : AC1 5) chain A residue 76 type sequence H description BINDING SITE FOR RESIDUE GOL A 200 source : AC1 6) chain A residue 77 type sequence S description BINDING SITE FOR RESIDUE GOL A 200 source : AC1 7) chain A residue 157 type sequence I description BINDING SITE FOR RESIDUE GOL A 200 source : AC1 8) chain A residue 160 type sequence L description BINDING SITE FOR RESIDUE GOL A 200 source : AC1 9) chain A residue 12 type catalytic sequence I description 518 source MCSA : MCSA1 10) chain A residue 77 type catalytic sequence S description 518 source MCSA : MCSA1 11) chain A residue 78 type catalytic sequence M description 518 source MCSA : MCSA1 12) chain A residue 133 type catalytic sequence D description 518 source MCSA : MCSA1 13) chain A residue 156 type catalytic sequence H description 518 source MCSA : MCSA1 14) chain A residue 77 type ACT_SITE sequence S description Nucleophile => ECO:0000305|PubMed:11491291, ECO:0000305|PubMed:11583117, ECO:0000305|PubMed:12077437 source Swiss-Prot : SWS_FT_FI1 15) chain A residue 133 type ACT_SITE sequence D description Charge relay system => ECO:0000305|PubMed:11491291, ECO:0000305|PubMed:11583117, ECO:0000305|PubMed:12077437 source Swiss-Prot : SWS_FT_FI2 16) chain A residue 156 type ACT_SITE sequence H description Charge relay system => ECO:0000305|PubMed:11491291, ECO:0000305|PubMed:11583117, ECO:0000305|PubMed:12077437 source Swiss-Prot : SWS_FT_FI2

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