eF-site ID 1qd6-C PDB Code 1qd6 Chain C click to enlarge Title OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI Classification MEMBRANE PROTEIN Compound OUTER MEMBRANE PHOSPHOLIPASE (OMPLA) Source Escherichia coli (strain K12) (PA1_ECOLI) Sequence C:  FTLYPYDTNYLIYTQTSDLNKEAIASYDWAENARKDEVKF QLSLAFPLWRGILGPNSVLGASYTQKSWWQLSNSEESSPF RETNYEPQLFLGFATDYRFAGWTLRDVEMGYNHDSNGRSD PTSRSWNRLYTRLMAENGNWLVEVKPWYVVGNTDDNPDIT KYMGYYQLKIGYHLGDAVLSAKGQYNWNTGYGGAELGLSY PITKHVRLYTQVYSGYGESLIDYNFNQTRVGVGVMLNDLF Description Functional site 1) chain C residue 147 type sequence R description BINDING SITE FOR RESIDUE CA C 1 source : AC1 2) chain C residue 152 type sequence S description BINDING SITE FOR RESIDUE CA C 1 source : AC1 3) chain C residue 106 type sequence S description BINDING SITE FOR RESIDUE CA C 2 source : AC2 4) chain C residue 92 type sequence Y description BINDING SITE FOR RESIDUE HDS C 270 source : AC3 5) chain C residue 114 type sequence Y description BINDING SITE FOR RESIDUE HDS C 270 source : AC3 6) chain C residue 142 type sequence H description BINDING SITE FOR RESIDUE HDS C 270 source : AC3 7) chain C residue 144 type sequence S description BINDING SITE FOR RESIDUE HDS C 270 source : AC3 8) chain C residue 145 type sequence N description BINDING SITE FOR RESIDUE HDS C 270 source : AC3 9) chain C residue 146 type sequence G description BINDING SITE FOR RESIDUE HDS C 270 source : AC3 10) chain C residue 39 type sequence Y description BINDING SITE FOR RESIDUE HDS D 270 source : AC4 11) chain C residue 71 type sequence L description BINDING SITE FOR RESIDUE HDS D 270 source : AC4 12) chain C residue 98 type sequence W description BINDING SITE FOR RESIDUE HDS D 270 source : AC4 13) chain C residue 109 type sequence F description BINDING SITE FOR RESIDUE HDS D 270 source : AC4 14) chain C residue 263 type sequence V description BINDING SITE FOR RESIDUE HDS D 270 source : AC4 15) chain C residue 265 type sequence L description BINDING SITE FOR RESIDUE HDS D 270 source : AC4 16) chain C residue 106 type catalytic sequence S description 650 source MCSA : MCSA1 17) chain C residue 142 type catalytic sequence H description 650 source MCSA : MCSA1 18) chain C residue 144 type catalytic sequence S description 650 source MCSA : MCSA1 19) chain C residue 146 type catalytic sequence G description 650 source MCSA : MCSA1 20) chain C residue 147 type catalytic sequence R description 650 source MCSA : MCSA1 21) chain C residue 152 type catalytic sequence S description 650 source MCSA : MCSA1 22) chain C residue 156 type catalytic sequence N description 650 source MCSA : MCSA1 23) chain C residue 33-45 type TRANSMEM sequence YPYDTNYLIYTQT description Beta stranded source Swiss-Prot : SWS_FT_FI1 24) chain C residue 222-230 type TRANSMEM sequence GAELGLSYP description Beta stranded source Swiss-Prot : SWS_FT_FI1 25) chain C residue 236-245 type TRANSMEM sequence RLYTQVYSGY description Beta stranded source Swiss-Prot : SWS_FT_FI1 26) chain C residue 255-266 type TRANSMEM sequence NQTRVGVGVMLN description Beta stranded source Swiss-Prot : SWS_FT_FI1 27) chain C residue 65-79 type TRANSMEM sequence DEVKFQLSLAFPLWR description Beta stranded source Swiss-Prot : SWS_FT_FI1 28) chain C residue 86-98 type TRANSMEM sequence SVLGASYTQKSWW description Beta stranded source Swiss-Prot : SWS_FT_FI1 29) chain C residue 109-128 type TRANSMEM sequence FRETNYEPQLFLGFATDYRF description Beta stranded source Swiss-Prot : SWS_FT_FI1 30) chain C residue 131-144 type TRANSMEM sequence WTLRDVEMGYNHDS description Beta stranded source Swiss-Prot : SWS_FT_FI1 31) chain C residue 154-166 type TRANSMEM sequence SWNRLYTRLMAEN description Beta stranded source Swiss-Prot : SWS_FT_FI1 32) chain C residue 169-178 type TRANSMEM sequence WLVEVKPWYV description Beta stranded source Swiss-Prot : SWS_FT_FI1 33) chain C residue 197-203 type TRANSMEM sequence LKIGYHL description Beta stranded source Swiss-Prot : SWS_FT_FI1 34) chain C residue 206-214 type TRANSMEM sequence AVLSAKGQY description Beta stranded source Swiss-Prot : SWS_FT_FI1 35) chain C residue 46-64 type TOPO_DOM sequence SDLNKEAIASYDWAENARK description Extracellular source Swiss-Prot : SWS_FT_FI2 36) chain C residue 99-108 type TOPO_DOM sequence QLSNSEESSP description Extracellular source Swiss-Prot : SWS_FT_FI2 37) chain C residue 145-153 type TOPO_DOM sequence NGRSDPTSR description Extracellular source Swiss-Prot : SWS_FT_FI2 38) chain C residue 179-196 type TOPO_DOM sequence VGNTDDNPDITKYMGYYQ description Extracellular source Swiss-Prot : SWS_FT_FI2 39) chain C residue 215-221 type TOPO_DOM sequence NWNTGYG description Extracellular source Swiss-Prot : SWS_FT_FI2 40) chain C residue 246-254 type TOPO_DOM sequence GESLIDYNF description Extracellular source Swiss-Prot : SWS_FT_FI2 41) chain C residue 80-85 type TOPO_DOM sequence GILGPN description Periplasmic source Swiss-Prot : SWS_FT_FI3 42) chain C residue 129-130 type TOPO_DOM sequence AG description Periplasmic source Swiss-Prot : SWS_FT_FI3 43) chain C residue 167-168 type TOPO_DOM sequence GN description Periplasmic source Swiss-Prot : SWS_FT_FI3 44) chain C residue 204-205 type TOPO_DOM sequence GD description Periplasmic source Swiss-Prot : SWS_FT_FI3 45) chain C residue 231-235 type TOPO_DOM sequence ITKHV description Periplasmic source Swiss-Prot : SWS_FT_FI3 46) chain C residue 267-269 type TOPO_DOM sequence DLF description Periplasmic source Swiss-Prot : SWS_FT_FI3 47) chain C residue 106 type BINDING sequence S description in dimeric form source Swiss-Prot : SWS_FT_FI6 48) chain C residue 147 type BINDING sequence R description in dimeric form source Swiss-Prot : SWS_FT_FI6 49) chain C residue 152 type BINDING sequence S description in dimeric form source Swiss-Prot : SWS_FT_FI6 50) chain C residue 184 type BINDING sequence D description in monomeric form source Swiss-Prot : SWS_FT_FI7 51) chain C residue 142 type ACT_SITE sequence H description Proton acceptor => ECO:0000305 source Swiss-Prot : SWS_FT_FI4 52) chain C residue 144 type ACT_SITE sequence S description Nucleophile => ECO:0000269|PubMed:2040286 source Swiss-Prot : SWS_FT_FI5

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