eF-site ID 1m9y-E PDB Code 1m9y Chain E 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 null (Q72497_9HIV1) Sequence E:  MVNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALS TGEKGFGYKGSCFHRIIPGFMCQGGDFTRHNGTGGKSIYG EKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTE WLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIAD CGQLE Description Functional site 1) 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 2) 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 3) chain E residue 28 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 4) chain E residue 82 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 5) chain E residue 44 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 6) chain E residue 76 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 7) chain E residue 131 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 8) chain E residue 77 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI5 9) chain E residue 93 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:20068231 source Swiss-Prot : SWS_FT_FI6 10) 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 11) chain E residue 133 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P17742 source Swiss-Prot : SWS_FT_FI8 12) chain E residue 108 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI9 13) 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 14) 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 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

Display surface Download Links