eF-site ID 1qd6-ABCD PDB Code 1qd6 Chain A, B, C, D click to enlarge Title OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI Classification MEMBRANE PROTEIN Compound OUTER MEMBRANE PHOSPHOLIPASE (OMPLA) Source null (PA1_ECOLI) Sequence A:  AVRGSIIANMLQE B:  AVRGSIIANMLQE C:  FTLYPYDTNYLIYTQTSDLNKEAIASYDWAENARKDEVKF QLSLAFPLWRGILGPNSVLGASYTQKSWWQLSNSEESSPF RETNYEPQLFLGFATDYRFAGWTLRDVEMGYNHDSNGRSD PTSRSWNRLYTRLMAENGNWLVEVKPWYVVGNTDDNPDIT KYMGYYQLKIGYHLGDAVLSAKGQYNWNTGYGGAELGLSY PITKHVRLYTQVYSGYGESLIDYNFNQTRVGVGVMLNDLF D:  TLYPYDTNYLIYTQTSDLNKEAIASYDWAENARKDEVKFQ LSLAFPLWRGILGPNSVLGASYTQKSWWQLSNSEESSPFR ETNYEPQLFLGFATDYRFAGWTLRDVEMGYNHDSNGRSDP TSRSWNRLYTRLMAENGNWLVEVKPWYVVGNTDDNPDITK YMGYYQLKIGYHLGDAVLSAKGQYNWNTGYGGAELGLSYP ITKHVRLYTQVYSGYGESLIDYNFNQTRVGVGVMLNDLF 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 D residue 106 type sequence S description BINDING SITE FOR RESIDUE CA C 1 source : AC1 4) chain C residue 106 type sequence S description BINDING SITE FOR RESIDUE CA C 2 source : AC2 5) chain D residue 147 type sequence R description BINDING SITE FOR RESIDUE CA C 2 source : AC2 6) chain D residue 152 type sequence S description BINDING SITE FOR RESIDUE CA C 2 source : AC2 7) chain C residue 92 type sequence Y description BINDING SITE FOR RESIDUE HDS C 270 source : AC3 8) chain C residue 114 type sequence Y description BINDING SITE FOR RESIDUE HDS C 270 source : AC3 9) chain C residue 142 type sequence H description BINDING SITE FOR RESIDUE HDS C 270 source : AC3 10) chain C residue 144 type sequence S description BINDING SITE FOR RESIDUE HDS C 270 source : AC3 11) chain C residue 145 type sequence N description BINDING SITE FOR RESIDUE HDS C 270 source : AC3 12) chain C residue 146 type sequence G description BINDING SITE FOR RESIDUE HDS C 270 source : AC3 13) chain D residue 39 type sequence Y description BINDING SITE FOR RESIDUE HDS C 270 source : AC3 14) chain D residue 69 type sequence F description BINDING SITE FOR RESIDUE HDS C 270 source : AC3 15) chain D residue 98 type sequence W description BINDING SITE FOR RESIDUE HDS C 270 source : AC3 16) chain D residue 109 type sequence F description BINDING SITE FOR RESIDUE HDS C 270 source : AC3 17) chain D residue 263 type sequence V description BINDING SITE FOR RESIDUE HDS C 270 source : AC3 18) chain D residue 265 type sequence L description BINDING SITE FOR RESIDUE HDS C 270 source : AC3 19) chain C residue 39 type sequence Y description BINDING SITE FOR RESIDUE HDS D 270 source : AC4 20) chain C residue 71 type sequence L description BINDING SITE FOR RESIDUE HDS D 270 source : AC4 21) chain C residue 98 type sequence W description BINDING SITE FOR RESIDUE HDS D 270 source : AC4 22) chain C residue 109 type sequence F description BINDING SITE FOR RESIDUE HDS D 270 source : AC4 23) chain C residue 263 type sequence V description BINDING SITE FOR RESIDUE HDS D 270 source : AC4 24) chain C residue 265 type sequence L description BINDING SITE FOR RESIDUE HDS D 270 source : AC4 25) chain D residue 92 type sequence Y description BINDING SITE FOR RESIDUE HDS D 270 source : AC4 26) chain D residue 142 type sequence H description BINDING SITE FOR RESIDUE HDS D 270 source : AC4 27) chain D residue 144 type sequence S description BINDING SITE FOR RESIDUE HDS D 270 source : AC4 28) chain D residue 145 type sequence N description BINDING SITE FOR RESIDUE HDS D 270 source : AC4 29) chain D residue 146 type sequence G description BINDING SITE FOR RESIDUE HDS D 270 source : AC4 30) chain D residue 142 type ACT_SITE sequence H description Proton acceptor => ECO:0000305 source Swiss-Prot : SWS_FT_FI4 31) chain C residue 142 type ACT_SITE sequence H description Proton acceptor => ECO:0000305 source Swiss-Prot : SWS_FT_FI4 32) chain D residue 144 type ACT_SITE sequence S description Nucleophile => ECO:0000269|PubMed:2040286 source Swiss-Prot : SWS_FT_FI5 33) chain C residue 144 type ACT_SITE sequence S description Nucleophile => ECO:0000269|PubMed:2040286 source Swiss-Prot : SWS_FT_FI5 34) chain C residue 106 type catalytic sequence S description 650 source MCSA : MCSA1 35) chain C residue 142 type catalytic sequence H description 650 source MCSA : MCSA1 36) chain C residue 144 type catalytic sequence S description 650 source MCSA : MCSA1 37) chain C residue 146 type catalytic sequence G description 650 source MCSA : MCSA1 38) chain C residue 147 type catalytic sequence R description 650 source MCSA : MCSA1 39) chain C residue 152 type catalytic sequence S description 650 source MCSA : MCSA1 40) chain C residue 156 type catalytic sequence N description 650 source MCSA : MCSA1 41) chain D residue 106 type catalytic sequence S description 650 source MCSA : MCSA2 42) chain D residue 142 type catalytic sequence H description 650 source MCSA : MCSA2 43) chain D residue 144 type catalytic sequence S description 650 source MCSA : MCSA2 44) chain D residue 146 type catalytic sequence G description 650 source MCSA : MCSA2 45) chain D residue 147 type catalytic sequence R description 650 source MCSA : MCSA2 46) chain D residue 152 type catalytic sequence S description 650 source MCSA : MCSA2 47) chain D residue 156 type catalytic sequence N description 650 source MCSA : MCSA2 48) chain C residue 33-45 type TRANSMEM sequence YPYDTNYLIYTQT description Beta stranded source Swiss-Prot : SWS_FT_FI1 49) chain C residue 65-79 type TRANSMEM sequence DEVKFQLSLAFPLWR description Beta stranded source Swiss-Prot : SWS_FT_FI1 50) chain C residue 86-98 type TRANSMEM sequence SVLGASYTQKSWW description Beta stranded source Swiss-Prot : SWS_FT_FI1 51) chain C residue 109-128 type TRANSMEM sequence FRETNYEPQLFLGFATDYRF description Beta stranded source Swiss-Prot : SWS_FT_FI1 52) chain C residue 131-144 type TRANSMEM sequence WTLRDVEMGYNHDS description Beta stranded source Swiss-Prot : SWS_FT_FI1 53) chain C residue 154-166 type TRANSMEM sequence SWNRLYTRLMAEN description Beta stranded source Swiss-Prot : SWS_FT_FI1 54) chain C residue 169-178 type TRANSMEM sequence WLVEVKPWYV description Beta stranded source Swiss-Prot : SWS_FT_FI1 55) chain C residue 197-203 type TRANSMEM sequence LKIGYHL description Beta stranded source Swiss-Prot : SWS_FT_FI1 56) chain C residue 206-214 type TRANSMEM sequence AVLSAKGQY description Beta stranded source Swiss-Prot : SWS_FT_FI1 57) chain C residue 222-230 type TRANSMEM sequence GAELGLSYP description Beta stranded source Swiss-Prot : SWS_FT_FI1 58) chain C residue 236-245 type TRANSMEM sequence RLYTQVYSGY description Beta stranded source Swiss-Prot : SWS_FT_FI1 59) chain C residue 255-266 type TRANSMEM sequence NQTRVGVGVMLN description Beta stranded source Swiss-Prot : SWS_FT_FI1 60) chain D residue 33-45 type TRANSMEM sequence YPYDTNYLIYTQT description Beta stranded source Swiss-Prot : SWS_FT_FI1 61) chain D residue 65-79 type TRANSMEM sequence DEVKFQLSLAFPLWR description Beta stranded source Swiss-Prot : SWS_FT_FI1 62) chain D residue 86-98 type TRANSMEM sequence SVLGASYTQKSWW description Beta stranded source Swiss-Prot : SWS_FT_FI1 63) chain D residue 109-128 type TRANSMEM sequence FRETNYEPQLFLGFATDYRF description Beta stranded source Swiss-Prot : SWS_FT_FI1 64) chain D residue 131-144 type TRANSMEM sequence WTLRDVEMGYNHDS description Beta stranded source Swiss-Prot : SWS_FT_FI1 65) chain D residue 154-166 type TRANSMEM sequence SWNRLYTRLMAEN description Beta stranded source Swiss-Prot : SWS_FT_FI1 66) chain D residue 169-178 type TRANSMEM sequence WLVEVKPWYV description Beta stranded source Swiss-Prot : SWS_FT_FI1 67) chain D residue 197-203 type TRANSMEM sequence LKIGYHL description Beta stranded source Swiss-Prot : SWS_FT_FI1 68) chain D residue 206-214 type TRANSMEM sequence AVLSAKGQY description Beta stranded source Swiss-Prot : SWS_FT_FI1 69) chain D residue 222-230 type TRANSMEM sequence GAELGLSYP description Beta stranded source Swiss-Prot : SWS_FT_FI1 70) chain D residue 236-245 type TRANSMEM sequence RLYTQVYSGY description Beta stranded source Swiss-Prot : SWS_FT_FI1 71) chain D residue 255-266 type TRANSMEM sequence NQTRVGVGVMLN description Beta stranded source Swiss-Prot : SWS_FT_FI1 72) chain C residue 46-64 type TOPO_DOM sequence SDLNKEAIASYDWAENARK description Extracellular source Swiss-Prot : SWS_FT_FI2 73) chain C residue 99-108 type TOPO_DOM sequence QLSNSEESSP description Extracellular source Swiss-Prot : SWS_FT_FI2 74) chain C residue 145-153 type TOPO_DOM sequence NGRSDPTSR description Extracellular source Swiss-Prot : SWS_FT_FI2 75) chain C residue 179-196 type TOPO_DOM sequence VGNTDDNPDITKYMGYYQ description Extracellular source Swiss-Prot : SWS_FT_FI2 76) chain C residue 215-221 type TOPO_DOM sequence NWNTGYG description Extracellular source Swiss-Prot : SWS_FT_FI2 77) chain C residue 246-254 type TOPO_DOM sequence GESLIDYNF description Extracellular source Swiss-Prot : SWS_FT_FI2 78) chain D residue 46-64 type TOPO_DOM sequence SDLNKEAIASYDWAENARK description Extracellular source Swiss-Prot : SWS_FT_FI2 79) chain D residue 99-108 type TOPO_DOM sequence QLSNSEESSP description Extracellular source Swiss-Prot : SWS_FT_FI2 80) chain D residue 145-153 type TOPO_DOM sequence NGRSDPTSR description Extracellular source Swiss-Prot : SWS_FT_FI2 81) chain D residue 179-196 type TOPO_DOM sequence VGNTDDNPDITKYMGYYQ description Extracellular source Swiss-Prot : SWS_FT_FI2 82) chain D residue 215-221 type TOPO_DOM sequence NWNTGYG description Extracellular source Swiss-Prot : SWS_FT_FI2 83) chain D residue 246-254 type TOPO_DOM sequence GESLIDYNF description Extracellular source Swiss-Prot : SWS_FT_FI2 84) chain C residue 80-85 type TOPO_DOM sequence GILGPN description Periplasmic source Swiss-Prot : SWS_FT_FI3 85) chain C residue 129-130 type TOPO_DOM sequence AG description Periplasmic source Swiss-Prot : SWS_FT_FI3 86) chain C residue 167-168 type TOPO_DOM sequence GN description Periplasmic source Swiss-Prot : SWS_FT_FI3 87) chain C residue 204-205 type TOPO_DOM sequence GD description Periplasmic source Swiss-Prot : SWS_FT_FI3 88) chain C residue 231-235 type TOPO_DOM sequence ITKHV description Periplasmic source Swiss-Prot : SWS_FT_FI3 89) chain C residue 267-269 type TOPO_DOM sequence DLF description Periplasmic source Swiss-Prot : SWS_FT_FI3 90) chain D residue 80-85 type TOPO_DOM sequence GILGPN description Periplasmic source Swiss-Prot : SWS_FT_FI3 91) chain D residue 129-130 type TOPO_DOM sequence AG description Periplasmic source Swiss-Prot : SWS_FT_FI3 92) chain D residue 167-168 type TOPO_DOM sequence GN description Periplasmic source Swiss-Prot : SWS_FT_FI3 93) chain D residue 204-205 type TOPO_DOM sequence GD description Periplasmic source Swiss-Prot : SWS_FT_FI3 94) chain D residue 231-235 type TOPO_DOM sequence ITKHV description Periplasmic source Swiss-Prot : SWS_FT_FI3 95) chain D residue 267-269 type TOPO_DOM sequence DLF description Periplasmic source Swiss-Prot : SWS_FT_FI3 96) chain C residue 147 type BINDING sequence R description in dimeric form source Swiss-Prot : SWS_FT_FI6 97) chain C residue 152 type BINDING sequence S description in dimeric form source Swiss-Prot : SWS_FT_FI6 98) chain D residue 106 type BINDING sequence S description in dimeric form source Swiss-Prot : SWS_FT_FI6 99) chain D residue 147 type BINDING sequence R description in dimeric form source Swiss-Prot : SWS_FT_FI6 100) chain D residue 152 type BINDING sequence S description in dimeric form source Swiss-Prot : SWS_FT_FI6 101) chain C residue 106 type BINDING sequence S description in dimeric form source Swiss-Prot : SWS_FT_FI6 102) chain C residue 184 type BINDING sequence D description in monomeric form source Swiss-Prot : SWS_FT_FI7 103) chain D residue 184 type BINDING sequence D description in monomeric form source Swiss-Prot : SWS_FT_FI7

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