eF-site ID 104l-AB PDB Code 104l Chain A, B click to enlarge Title HOW AMINO-ACID INSERTIONS ARE ALLOWED IN AN ALPHA-HELIX OF T4 LYSOZYME Classification HYDROLASE(O-GLYCOSYL) Compound T4 LYSOZYME Source null (LYS_BPT4) Sequence A:  MNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLN AAKSAAELDKAIGRNTNGVITKDEAEKLFNQDVDAAVRGI LRNAKLKPVYDSLDAVRRAALINMVFQMGETGVAGFTNSL RMLQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTW DAYK B:  MNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLN AAKSAAELDKAIGRNTNGVITKDEAEKLFNQDVDAAVRGI LRNAKLKPVYDSLDAVRRAALINMVFQMGETGVAGFTNSL RMLQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTW DAYK Description Functional site 1) chain A residue 11 type catalytic sequence E description 921 source MCSA : MCSA1 2) chain A residue 20 type catalytic sequence D description 921 source MCSA : MCSA1 3) chain B residue 11 type catalytic sequence E description 921 source MCSA : MCSA2 4) chain B residue 20 type catalytic sequence D description 921 source MCSA : MCSA2 5) chain A residue 32 type BINDING sequence L description BINDING => ECO:0000269|PubMed:8266098 source Swiss-Prot : SWS_FT_FI3 6) chain B residue 32 type BINDING sequence L description BINDING => ECO:0000269|PubMed:8266098 source Swiss-Prot : SWS_FT_FI3 7) chain B residue 102 type BINDING sequence M description BINDING => ECO:0000269|PubMed:8266098 source Swiss-Prot : SWS_FT_FI3 8) chain A residue 102 type BINDING sequence M description BINDING => ECO:0000269|PubMed:8266098 source Swiss-Prot : SWS_FT_FI3 9) chain B residue 115 type BINDING sequence T description BINDING => ECO:0000303|PubMed:7831309 source Swiss-Prot : SWS_FT_FI4 10) chain B residue 130 type BINDING sequence A description BINDING => ECO:0000303|PubMed:7831309 source Swiss-Prot : SWS_FT_FI4 11) chain A residue 115 type BINDING sequence T description BINDING => ECO:0000303|PubMed:7831309 source Swiss-Prot : SWS_FT_FI4 12) chain A residue 130 type BINDING sequence A description BINDING => ECO:0000303|PubMed:7831309 source Swiss-Prot : SWS_FT_FI4 13) chain B residue 11 type ACT_SITE sequence E description Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098 source Swiss-Prot : SWS_FT_FI1 14) chain A residue 11 type ACT_SITE sequence E description Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098 source Swiss-Prot : SWS_FT_FI1 15) chain A residue 20 type ACT_SITE sequence D description Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:1892846, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098 source Swiss-Prot : SWS_FT_FI2 16) chain B residue 20 type ACT_SITE sequence D description Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:1892846, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098 source Swiss-Prot : SWS_FT_FI2

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