eF-site ID 1c6m-A PDB Code 1c6m Chain A click to enlarge Title T4 LYSOZYME MUTANT C54T/C97A/L99A/F153A IN THE PRESENCE OF 8 ATM KRYPTON Classification HYDROLASE Compound PROTEIN (LYSOZYME) Source Enterobacteria phage T4 (Bacteriophage T4) (LYCV_BPT4) Sequence A:  MNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLN AAKSELDKAIGRNTNGVITKDEAEKLFNQDVDAAVRGILR NAKLKPVYDSLDAVRRAAAINMVFQMGETGVAGFTNSLRM LQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTARTGTWDA YK Description Functional site 1) chain A residue 142 type sequence T description BINDING SITE FOR RESIDUE CL A 173 source : AC1 2) chain A residue 144 type sequence N description BINDING SITE FOR RESIDUE CL A 173 source : AC1 3) chain A residue 145 type sequence R description BINDING SITE FOR RESIDUE CL A 173 source : AC1 4) chain A residue 118 type sequence L description BINDING SITE FOR RESIDUE KR A 501 source : AC3 5) chain A residue 98 type sequence A description BINDING SITE FOR RESIDUE KR A 502 source : AC4 6) chain A residue 99 type sequence A description BINDING SITE FOR RESIDUE KR A 502 source : AC4 7) chain A residue 126 type sequence W description BINDING SITE FOR RESIDUE KR A 503 source : AC5 8) chain A residue 129 type sequence A description BINDING SITE FOR RESIDUE KR A 503 source : AC5 9) chain A residue 130 type sequence A description BINDING SITE FOR RESIDUE KR A 503 source : AC5 10) chain A residue 153 type sequence A description BINDING SITE FOR RESIDUE KR A 503 source : AC5 11) chain A residue 154 type sequence R description BINDING SITE FOR RESIDUE KR A 503 source : AC5 12) chain A residue 72 type sequence D description BINDING SITE FOR RESIDUE BME A 901 source : AC6 13) chain A residue 68 type sequence N description BINDING SITE FOR RESIDUE BME A 902 source : AC7 14) chain A residue 72 type sequence D description BINDING SITE FOR RESIDUE BME A 902 source : AC7 15) chain A residue 93 type sequence A description BINDING SITE FOR RESIDUE BME A 902 source : AC7 16) 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 17) 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 18) chain A residue 11 type catalytic sequence E description 921 source MCSA : MCSA1 19) chain A residue 20 type catalytic sequence D description 921 source MCSA : MCSA1 20) chain A residue 117 type BINDING sequence S description BINDING => ECO:0000303|PubMed:7831309 source Swiss-Prot : SWS_FT_FI4 21) chain A residue 132 type BINDING sequence N description BINDING => ECO:0000303|PubMed:7831309 source Swiss-Prot : SWS_FT_FI4 22) chain A residue 32 type BINDING sequence L description BINDING => ECO:0000269|PubMed:8266098 source Swiss-Prot : SWS_FT_FI3 23) chain A residue 104 type BINDING sequence F description BINDING => ECO:0000269|PubMed:8266098 source Swiss-Prot : SWS_FT_FI3

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