eF-site ID 172l-A PDB Code 172l Chain A click to enlarge Title PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF T4 LYSOZYME Classification HYDROLASE (O-GLYCOSYL) Compound T4 LYSOZYME Source Enterobacteria phage T4 (Bacteriophage T4) (LYS_BPT4) Sequence A:  MNCFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLN AAKSELDKAIGRNCNGVITKDEAEKLFNQDVDAAVRGILR NAKLKPVYDSLDAVRRCALINMVFQMGETGVAGFTNSLRM LQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDA YKNL Description (1)  LYSOZYME (E.C.3.2.1.17) MUTANT WITH ILE 3 REPLACED BY CYS (I3C) Functional site 1) chain A residue 6 type sequence M description COMPRISES RESIDUES WITHIN 8 ANGSTROMS OF ATOM SG CYS 3 source : I3C 2) chain A residue 7 type sequence L description COMPRISES RESIDUES WITHIN 8 ANGSTROMS OF ATOM SG CYS 3 source : I3C 3) chain A residue 67 type sequence F description COMPRISES RESIDUES WITHIN 8 ANGSTROMS OF ATOM SG CYS 3 source : I3C 4) chain A residue 71 type sequence V description COMPRISES RESIDUES WITHIN 8 ANGSTROMS OF ATOM SG CYS 3 source : I3C 5) chain A residue 94 type sequence V description COMPRISES RESIDUES WITHIN 8 ANGSTROMS OF ATOM SG CYS 3 source : I3C 6) chain A residue 96 type sequence R description COMPRISES RESIDUES WITHIN 8 ANGSTROMS OF ATOM SG CYS 3 source : I3C 7) chain A residue 97 type sequence C description COMPRISES RESIDUES WITHIN 8 ANGSTROMS OF ATOM SG CYS 3 source : I3C 8) chain A residue 100 type sequence I description COMPRISES RESIDUES WITHIN 8 ANGSTROMS OF ATOM SG CYS 3 source : I3C 9) chain A residue 101 type sequence N description COMPRISES RESIDUES WITHIN 8 ANGSTROMS OF ATOM SG CYS 3 source : I3C 10) chain A residue 158 type sequence W description COMPRISES RESIDUES WITHIN 8 ANGSTROMS OF ATOM SG CYS 3 source : I3C 11) chain A residue 50 type sequence I description BINDING SITE FOR RESIDUE BME A 170 source : AC1 12) chain A residue 52 type sequence R description BINDING SITE FOR RESIDUE BME A 170 source : AC1 13) chain A residue 53 type sequence N description BINDING SITE FOR RESIDUE BME A 170 source : AC1 14) chain A residue 54 type sequence C description BINDING SITE FOR RESIDUE BME A 170 source : AC1 15) chain A residue 57 type sequence V description BINDING SITE FOR RESIDUE BME A 170 source : AC1 16) chain A residue 58 type sequence I description BINDING SITE FOR RESIDUE BME A 170 source : AC1 17) chain A residue 59 type sequence T description BINDING SITE FOR RESIDUE BME A 170 source : AC1 18) chain A residue 62 type sequence E description BINDING SITE FOR RESIDUE BME A 170 source : AC1 19) chain A residue 11 type catalytic sequence E description 921 source MCSA : MCSA1 20) chain A residue 20 type catalytic sequence D description 921 source MCSA : MCSA1 21) 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 22) 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 23) chain A residue 32 type BINDING sequence L description BINDING => ECO:0000269|PubMed:8266098 source Swiss-Prot : SWS_FT_FI3 24) chain A residue 104 type BINDING sequence F description BINDING => ECO:0000269|PubMed:8266098 source Swiss-Prot : SWS_FT_FI3 25) chain A residue 117 type BINDING sequence S description BINDING => ECO:0000303|PubMed:7831309 source Swiss-Prot : SWS_FT_FI4 26) chain A residue 132 type BINDING sequence N description BINDING => ECO:0000303|PubMed:7831309 source Swiss-Prot : SWS_FT_FI4

Display surface Download Links