eF-site ID 4tn3-A PDB Code 4tn3 Chain A click to enlarge Title Structure of the BBox-Coiled-coil region of Rhesus Trim5alpha Classification ANTIVIRAL PROTEIN Compound TRIM5/cyclophilin A fusion protein/T4 Lysozyme chimera Source (ENLYS_BPT4) Sequence A:  VDHCARHGEKLLLFCQEDSKVICWLCKDSQEHRGHHTFLM EEVAQEYHVKLQTALEMLRQKQQEAEKLEADIREEKASWK IQIDYDKTNVSADFEQLREILDWEESNELQNLEKEEEDIL KSLTKSETEMVQQTQYMRELISELEHRLQMMDLLQGVDGI IKRIENMTLFRAPDLKGMLDMFRDAAAEESPVLLAMNIFE MLRIDEGLRLKIYKNTEGYYTIGIGHLLTKSPSLNAAKSE LDKAIGRNTNGVITKDEAEKLFNQDVDAAVRGILRNAKLK PVYDSLDAVRRAALINMVFQMGETGVAGFTNSLRMLQQKR WDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDAYKNL Description Functional site 1) chain A residue 108 type sequence C description binding site for residue ZN A 701 source : AC1 2) chain A residue 111 type sequence D description binding site for residue ZN A 701 source : AC1 3) chain A residue 124 type sequence E description binding site for residue ZN A 701 source : AC1 4) chain A residue 125 type sequence H description binding site for residue ZN A 701 source : AC1 5) chain A residue 128 type sequence H description binding site for residue ZN A 701 source : AC1 6) chain A residue 97 type sequence C description binding site for residue ZN A 702 source : AC2 7) chain A residue 100 type sequence H description binding site for residue ZN A 702 source : AC2 8) chain A residue 116 type sequence C description binding site for residue ZN A 702 source : AC2 9) chain A residue 119 type sequence C description binding site for residue ZN A 702 source : AC2 10) chain A residue 335 type BINDING sequence L description BINDING => ECO:0000269|PubMed:8266098 source Swiss-Prot : SWS_FT_FI3 11) chain A residue 407 type BINDING sequence F description BINDING => ECO:0000269|PubMed:8266098 source Swiss-Prot : SWS_FT_FI3 12) chain A residue 420 type BINDING sequence S description BINDING => ECO:0000303|PubMed:7831309 source Swiss-Prot : SWS_FT_FI4 13) chain A residue 435 type BINDING sequence N description BINDING => ECO:0000303|PubMed:7831309 source Swiss-Prot : SWS_FT_FI4 14) chain A residue 314 type ACT_SITE sequence E description Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098 source Swiss-Prot : SWS_FT_FI1 15) chain A residue 323 type ACT_SITE sequence N description Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:1892846, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098 source Swiss-Prot : SWS_FT_FI2 16) chain A residue 314 type catalytic sequence E description 921 source MCSA : MCSA1 17) chain A residue 323 type catalytic sequence N description 921 source MCSA : MCSA1

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