eF-site ID 5ckr-A PDB Code 5ckr Chain A click to enlarge Title Crystal Structure of MraY in complex with Muraymycin D2 Classification TRANSFERASE/ANTIBIOTIC Compound Phospho-N-acetylmuramoyl-pentapeptide-transferase Source (MRAY_AQUAE) Sequence A:  KYITFRSFTAVLIAFFLTLVLSPSFINRLRKIQRLFGGVK KYTPTMGGIVILIVVTLSTLLLMRWDIKYTWVVLLSFLSF GTIGFWDDYVKLKNKKGISIKTKFLLQVLSASLISVLIYY WADIDTILYFPFFKELYVDLGVLYLPFAVFVIVGSANAVN LTDGLDGLAIGPAMTTATALGVVAYAVGHSKIAQYLNIPY VPYAGELTVFCFALVGAGLGFLWFNSFPAQMFMGDVGSLS IGASLATVALLTKSEFIFAVAAGVFVFETISVILQIIYFR WTGGKRLFKRAPFHHHLELNGLPEPKIVVRMWIISILLAI IAISMLKLR Description Functional site 1) chain A residue 70 type sequence K description binding site for residue 57M A 401 source : AC1 2) chain A residue 75 type sequence T description binding site for residue 57M A 401 source : AC1 3) chain A residue 190 type sequence N description binding site for residue 57M A 401 source : AC1 4) chain A residue 193 type sequence D description binding site for residue 57M A 401 source : AC1 5) chain A residue 194 type sequence G description binding site for residue 57M A 401 source : AC1 6) chain A residue 195 type sequence L description binding site for residue 57M A 401 source : AC1 7) chain A residue 196 type sequence D description binding site for residue 57M A 401 source : AC1 8) chain A residue 255 type sequence N description binding site for residue 57M A 401 source : AC1 9) chain A residue 262 type sequence F description binding site for residue 57M A 401 source : AC1 10) chain A residue 263 type sequence M description binding site for residue 57M A 401 source : AC1 11) chain A residue 264 type sequence G description binding site for residue 57M A 401 source : AC1 12) chain A residue 265 type sequence D description binding site for residue 57M A 401 source : AC1 13) chain A residue 268 type sequence S description binding site for residue 57M A 401 source : AC1 14) chain A residue 302 type sequence V description binding site for residue 57M A 401 source : AC1 15) chain A residue 305 type sequence Q description binding site for residue 57M A 401 source : AC1 16) chain A residue 320 type sequence R description binding site for residue 57M A 401 source : AC1 17) chain A residue 321 type sequence A description binding site for residue 57M A 401 source : AC1 18) chain A residue 322 type sequence P description binding site for residue 57M A 401 source : AC1 19) chain A residue 325 type sequence H description binding site for residue 57M A 401 source : AC1 20) chain A residue 93-98 type TOPO_DOM sequence MRWDIK description Periplasmic => ECO:0000269|PubMed:23990562 source Swiss-Prot : SWS_FT_FI1 21) chain A residue 153-172 type TOPO_DOM sequence DIDTILYFPFFKELYVDLGV description Periplasmic => ECO:0000269|PubMed:23990562 source Swiss-Prot : SWS_FT_FI1 22) chain A residue 219-233 type TOPO_DOM sequence HSKIAQYLNIPYVPY description Periplasmic => ECO:0000269|PubMed:23990562 source Swiss-Prot : SWS_FT_FI1 23) chain A residue 281-284 type TOPO_DOM sequence LTKS description Periplasmic => ECO:0000269|PubMed:23990562 source Swiss-Prot : SWS_FT_FI1 24) chain A residue 356-359 type TOPO_DOM sequence LKLR description Periplasmic => ECO:0000269|PubMed:23990562 source Swiss-Prot : SWS_FT_FI1 25) chain A residue 26-48 type TRANSMEM sequence SFTAVLIAFFLTLVLSPSFINRL description Helical; Name=Helix 1 => ECO:0000269|PubMed:23990562 source Swiss-Prot : SWS_FT_FI2 26) chain A residue 49-74 type TOPO_DOM sequence RKIQRLFGGVKKYTP description Cytoplasmic => ECO:0000269|PubMed:23990562 source Swiss-Prot : SWS_FT_FI3 27) chain A residue 121-130 type TOPO_DOM sequence KLKNKKGISI description Cytoplasmic => ECO:0000269|PubMed:23990562 source Swiss-Prot : SWS_FT_FI3 28) chain A residue 195-197 type TOPO_DOM sequence LDG description Cytoplasmic => ECO:0000269|PubMed:23990562 source Swiss-Prot : SWS_FT_FI3 29) chain A residue 256-264 type TOPO_DOM sequence SFPAQMFMG description Cytoplasmic => ECO:0000269|PubMed:23990562 source Swiss-Prot : SWS_FT_FI3 30) chain A residue 311-332 type TOPO_DOM sequence WTGGKRLFKRAPFHHHLELNGL description Cytoplasmic => ECO:0000269|PubMed:23990562 source Swiss-Prot : SWS_FT_FI3 31) chain A residue 75-92 type TRANSMEM sequence TMGGIVILIVVTLSTLLL description Helical; Name=Helix 2 => ECO:0000269|PubMed:23990562 source Swiss-Prot : SWS_FT_FI4 32) chain A residue 99-120 type TRANSMEM sequence YTWVVLLSFLSFGTIGFWDDYV description Helical; Name=Helix 3 => ECO:0000269|PubMed:23990562 source Swiss-Prot : SWS_FT_FI5 33) chain A residue 131-152 type TRANSMEM sequence KTKFLLQVLSASLISVLIYYWA description Helical; Name=Helix 4 => ECO:0000269|PubMed:23990562 source Swiss-Prot : SWS_FT_FI6 34) chain A residue 173-194 type TRANSMEM sequence LYLPFAVFVIVGSANAVNLTDG description Helical; Name=Helix 5 => ECO:0000269|PubMed:23990562 source Swiss-Prot : SWS_FT_FI7 35) chain A residue 198-218 type TRANSMEM sequence LAIGPAMTTATALGVVAYAVG description Helical; Name=Helix 6 => ECO:0000269|PubMed:23990562 source Swiss-Prot : SWS_FT_FI8 36) chain A residue 234-255 type TRANSMEM sequence AGELTVFCFALVGAGLGFLWFN description Helical; Name=Helix 7 => ECO:0000269|PubMed:23990562 source Swiss-Prot : SWS_FT_FI9 37) chain A residue 265-280 type TRANSMEM sequence DVGSLSIGASLATVAL description Helical; Name=Helix 8 => ECO:0000269|PubMed:23990562 source Swiss-Prot : SWS_FT_FI10 38) chain A residue 285-310 type TRANSMEM sequence EFIFAVAAGVFVFETISVILQIIYFR description Helical; Name=Helix 9 => ECO:0000269|PubMed:23990562 source Swiss-Prot : SWS_FT_FI11 39) chain A residue 333-355 type TRANSMEM sequence PEPKIVVRMWIISILLAIIAISM description Helical; Name=Helix 10 => ECO:0000269|PubMed:23990562 source Swiss-Prot : SWS_FT_FI12 40) chain A residue 305 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:27088606, ECO:0007744|PDB:5CKR source Swiss-Prot : SWS_FT_FI13 41) chain A residue 321 type BINDING sequence A description BINDING => ECO:0000269|PubMed:27088606, ECO:0007744|PDB:5CKR source Swiss-Prot : SWS_FT_FI13 42) chain A residue 70 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27088606, ECO:0007744|PDB:5CKR source Swiss-Prot : SWS_FT_FI13 43) chain A residue 75 type BINDING sequence T description BINDING => ECO:0000269|PubMed:27088606, ECO:0007744|PDB:5CKR source Swiss-Prot : SWS_FT_FI13 44) chain A residue 190 type BINDING sequence N description BINDING => ECO:0000269|PubMed:27088606, ECO:0007744|PDB:5CKR source Swiss-Prot : SWS_FT_FI13 45) chain A residue 193 type BINDING sequence D description BINDING => ECO:0000269|PubMed:27088606, ECO:0007744|PDB:5CKR source Swiss-Prot : SWS_FT_FI13 46) chain A residue 196 type BINDING sequence D description BINDING => ECO:0000269|PubMed:27088606, ECO:0007744|PDB:5CKR source Swiss-Prot : SWS_FT_FI13 47) chain A residue 264 type BINDING sequence G description BINDING => ECO:0000269|PubMed:27088606, ECO:0007744|PDB:5CKR source Swiss-Prot : SWS_FT_FI13 48) chain A residue 268 type BINDING sequence S description BINDING => ECO:0000269|PubMed:27088606, ECO:0007744|PDB:5CKR source Swiss-Prot : SWS_FT_FI13 49) chain A residue 70-82 type prosite sequence KKYTPTMGGIVIL description MRAY_1 MraY family signature 1. KkyTPTMGGIvIL source prosite : PS01347 50) chain A residue 187-198 type prosite sequence NAVNLTDGLDGL description MRAY_2 MraY family signature 2. NavNlTDGLDGL source prosite : PS01348

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