eF-site ID 1m9y-ABCDEFGH PDB Code 1m9y Chain A, B, C, D, E, F, G, H click to enlarge Title X-ray crystal structure of Cyclophilin A/HIV-1 CA N-terminal domain (1-146) M-type H87A,G89A Complex. Classification Isomerase/Viral protein Compound Cyclophilin A Source Homo sapiens (Human) (Q72497_9HIV1) Sequence A:  MVNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALS TGEKGFGYKGSCFHRIIPGFMCQGGDFTRHNGTGGKSIYG EKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTE WLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIAD CGQLE B:  VNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALST GEKGFGYKGSCFHRIIPGFMCQGGDFTRHNGTGGKSIYGE KFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEW LDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIADC GQLE C:  PIVQNLQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMF SALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEW DRLHPVAAAPIAPGQMREPRGSDIAGTTSTLQEQIGWMTH NPPIPVGEIYKRWIILGLNKIVRMYS D:  HQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQD LNTMLNTVGGHQAAMQMLKETINEEAAEWDRLHPVAAAPI APGQMREPRGSDIAGTTSTLQEQIGWMTHNPPIPVGEIYK RWIILGLNKIVRMYS E:  MVNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALS TGEKGFGYKGSCFHRIIPGFMCQGGDFTRHNGTGGKSIYG EKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTE WLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIAD CGQLE F:  VNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALST GEKGFGYKGSCFHRIIPGFMCQGGDFTRHNGTGGKSIYGE KFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEW LDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIADC GQLE G:  PIVQNLQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMF SALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEW DRLHPVAAAPIAPGQMREPRGSDIAGTTSTLQEQIGWMTH NPPIPVGEIYKRWIILGLNKIVRMYS H:  HQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQD LNTMLNTVGGHQAAMQMLKETINEEAAEWDRLHPVAAAPI APGQMREPRGSDIAGTTSTLQEQIGWMTHNPPIPVGEIYK RWIILGLNKIVRMYS Description Functional site 1) chain A residue 55 type catalytic sequence R description 189 source MCSA : MCSA1 2) chain A residue 60 type catalytic sequence F description 189 source MCSA : MCSA1 3) chain A residue 63 type catalytic sequence Q description 189 source MCSA : MCSA1 4) chain A residue 102 type catalytic sequence N description 189 source MCSA : MCSA1 5) chain A residue 113 type catalytic sequence F description 189 source MCSA : MCSA1 6) chain A residue 122 type catalytic sequence L description 189 source MCSA : MCSA1 7) chain A residue 126 type catalytic sequence H description 189 source MCSA : MCSA1 8) chain B residue 55 type catalytic sequence R description 189 source MCSA : MCSA2 9) chain B residue 60 type catalytic sequence F description 189 source MCSA : MCSA2 10) chain B residue 63 type catalytic sequence Q description 189 source MCSA : MCSA2 11) chain B residue 102 type catalytic sequence N description 189 source MCSA : MCSA2 12) chain B residue 113 type catalytic sequence F description 189 source MCSA : MCSA2 13) chain B residue 122 type catalytic sequence L description 189 source MCSA : MCSA2 14) chain B residue 126 type catalytic sequence H description 189 source MCSA : MCSA2 15) chain E residue 55 type catalytic sequence R description 189 source MCSA : MCSA3 16) chain E residue 60 type catalytic sequence F description 189 source MCSA : MCSA3 17) chain E residue 63 type catalytic sequence Q description 189 source MCSA : MCSA3 18) chain E residue 102 type catalytic sequence N description 189 source MCSA : MCSA3 19) chain E residue 113 type catalytic sequence F description 189 source MCSA : MCSA3 20) chain E residue 122 type catalytic sequence L description 189 source MCSA : MCSA3 21) chain E residue 126 type catalytic sequence H description 189 source MCSA : MCSA3 22) chain F residue 55 type catalytic sequence R description 189 source MCSA : MCSA4 23) chain F residue 60 type catalytic sequence F description 189 source MCSA : MCSA4 24) chain F residue 63 type catalytic sequence Q description 189 source MCSA : MCSA4 25) chain F residue 102 type catalytic sequence N description 189 source MCSA : MCSA4 26) chain F residue 113 type catalytic sequence F description 189 source MCSA : MCSA4 27) chain F residue 122 type catalytic sequence L description 189 source MCSA : MCSA4 28) chain F residue 126 type catalytic sequence H description 189 source MCSA : MCSA4 29) chain A residue 48-65 type prosite sequence YKGSCFHRIIPGFMCQGG description CSA_PPIASE_1 Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature. YkgScFHRIIpgFMcQGG source prosite : PS00170 30) chain A residue 1 type MOD_RES sequence M description N-acetylmethionine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712 source Swiss-Prot : SWS_FT_FI1 31) chain E residue 1 type MOD_RES sequence M description N-acetylmethionine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712 source Swiss-Prot : SWS_FT_FI1 32) chain A residue 28 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate source Swiss-Prot : SWS_FT_FI10 33) chain B residue 28 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate source Swiss-Prot : SWS_FT_FI10 34) chain E residue 28 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate source Swiss-Prot : SWS_FT_FI10 35) chain F residue 28 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate source Swiss-Prot : SWS_FT_FI10 36) chain A residue 82 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI11 37) chain B residue 82 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI11 38) chain E residue 82 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI11 39) chain F residue 82 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI11 40) chain A residue 2 type MOD_RES sequence V description N-acetylvaline; partial; in Peptidyl-prolyl cis-trans isomerase A, N-terminally processed => ECO:0000269|PubMed:25489052, ECO:0000269|Ref.12, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:25944712 source Swiss-Prot : SWS_FT_FI2 41) chain B residue 2 type MOD_RES sequence V description N-acetylvaline; partial; in Peptidyl-prolyl cis-trans isomerase A, N-terminally processed => ECO:0000269|PubMed:25489052, ECO:0000269|Ref.12, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:25944712 source Swiss-Prot : SWS_FT_FI2 42) chain E residue 2 type MOD_RES sequence V description N-acetylvaline; partial; in Peptidyl-prolyl cis-trans isomerase A, N-terminally processed => ECO:0000269|PubMed:25489052, ECO:0000269|Ref.12, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:25944712 source Swiss-Prot : SWS_FT_FI2 43) chain F residue 2 type MOD_RES sequence V description N-acetylvaline; partial; in Peptidyl-prolyl cis-trans isomerase A, N-terminally processed => ECO:0000269|PubMed:25489052, ECO:0000269|Ref.12, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:25944712 source Swiss-Prot : SWS_FT_FI2 44) chain A residue 28 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 45) chain A residue 82 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 46) chain B residue 28 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 47) chain B residue 82 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 48) chain E residue 28 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 49) chain E residue 82 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 50) chain F residue 28 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 51) chain F residue 82 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 52) chain A residue 44 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 53) chain F residue 44 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 54) chain F residue 76 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 55) chain F residue 131 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 56) chain A residue 76 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 57) chain A residue 131 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 58) chain B residue 44 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 59) chain B residue 76 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 60) chain B residue 131 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 61) chain E residue 44 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 62) chain E residue 76 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 63) chain E residue 131 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 64) chain A residue 77 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI5 65) chain B residue 77 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI5 66) chain E residue 77 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI5 67) chain F residue 77 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI5 68) chain A residue 93 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:20068231 source Swiss-Prot : SWS_FT_FI6 69) chain B residue 93 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:20068231 source Swiss-Prot : SWS_FT_FI6 70) chain E residue 93 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:20068231 source Swiss-Prot : SWS_FT_FI6 71) chain F residue 93 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:20068231 source Swiss-Prot : SWS_FT_FI6 72) chain A residue 125 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:20364129, ECO:0000269|PubMed:25678563, ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 73) chain B residue 125 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:20364129, ECO:0000269|PubMed:25678563, ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 74) chain E residue 125 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:20364129, ECO:0000269|PubMed:25678563, ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 75) chain F residue 125 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:20364129, ECO:0000269|PubMed:25678563, ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 76) chain A residue 133 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P17742 source Swiss-Prot : SWS_FT_FI8 77) chain B residue 133 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P17742 source Swiss-Prot : SWS_FT_FI8 78) chain E residue 133 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P17742 source Swiss-Prot : SWS_FT_FI8 79) chain F residue 133 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P17742 source Swiss-Prot : SWS_FT_FI8 80) chain A residue 108 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI9 81) chain B residue 108 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI9 82) chain E residue 108 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI9 83) chain F residue 108 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI9

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