eF-site ID 3prm-ABCD PDB Code 3prm Chain A, B, C, D click to enlarge Title Structural analysis of a viral OTU domain protease from the Crimean-Congo Hemorrhagic Fever virus in complex with human ubiquitin Classification HYDROLASE/HYDROLASE Compound RNA-directed RNA polymerase L Source Homo sapiens (Human) (J3QS39_HUMAN) Sequence A:  DFLRSLDWTQVIAGQYVSNPRFNISDYFEIVRQPGDGNCF YHSIAELTXPNKTDHSYHYIKRLTESAARKYYQEEPEARL VGLSLEDYLKRXLSDNEWGSTLEASXLAKEXGITIIIWTV AASDEVEAGIKFGDGDVFTAVNLLHSGQTHFDALRILPQF E B:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGX C:  DFLRSLDWTQVIAGQYVSNPRFNISDYFEIVRQPGDGNCF YHSIAELTXPNKTDHSYHYIKRLTESAARKYYQEEPEARL VGLSLEDYLKRXLSDNEWGSTLEASXLAKEXGITIIIWTV AASDEVEAGIKFGDGDVFTAVNLLHSGQTHFDALRILPQF E D:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGX Description Functional site 1) chain A residue 38 type sequence G description BINDING SITE FOR RESIDUE 4LJ B 76 source : AC1 2) chain A residue 40 type sequence C description BINDING SITE FOR RESIDUE 4LJ B 76 source : AC1 3) chain A residue 99 type sequence W description BINDING SITE FOR RESIDUE 4LJ B 76 source : AC1 4) chain A residue 150 type sequence T description BINDING SITE FOR RESIDUE 4LJ B 76 source : AC1 5) chain A residue 151 type sequence H description BINDING SITE FOR RESIDUE 4LJ B 76 source : AC1 6) chain B residue 48 type sequence K description BINDING SITE FOR RESIDUE 4LJ B 76 source : AC1 7) chain B residue 75 type sequence G description BINDING SITE FOR RESIDUE 4LJ B 76 source : AC1 8) chain C residue 40 type sequence C description BINDING SITE FOR RESIDUE 4LJ D 76 source : AC2 9) chain C residue 99 type sequence W description BINDING SITE FOR RESIDUE 4LJ D 76 source : AC2 10) chain C residue 150 type sequence T description BINDING SITE FOR RESIDUE 4LJ D 76 source : AC2 11) chain D residue 75 type sequence G description BINDING SITE FOR RESIDUE 4LJ D 76 source : AC2 12) chain B residue 27-52 type prosite sequence KAKIQDKEGIPPDQQRLIFAGKQLED description UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD source prosite : PS00299 13) chain A residue 40 type ACT_SITE sequence C description For ubiquitin thioesterase activity => ECO:0000269|PubMed:21228232, ECO:0000269|PubMed:21266548 source Swiss-Prot : SWS_FT_FI1 14) chain A residue 153 type ACT_SITE sequence D description For ubiquitin thioesterase activity => ECO:0000269|PubMed:21228232, ECO:0000269|PubMed:21266548 source Swiss-Prot : SWS_FT_FI1 15) chain C residue 40 type ACT_SITE sequence C description For ubiquitin thioesterase activity => ECO:0000269|PubMed:21228232, ECO:0000269|PubMed:21266548 source Swiss-Prot : SWS_FT_FI1 16) chain C residue 153 type ACT_SITE sequence D description For ubiquitin thioesterase activity => ECO:0000269|PubMed:21228232, ECO:0000269|PubMed:21266548 source Swiss-Prot : SWS_FT_FI1 17) chain A residue 151 type ACT_SITE sequence H description For ubiquitin thioesterase activity => ECO:0000269|PubMed:21228232, ECO:0000269|PubMed:21266548, ECO:0000305|PubMed:18078692 source Swiss-Prot : SWS_FT_FI2 18) chain C residue 151 type ACT_SITE sequence H description For ubiquitin thioesterase activity => ECO:0000269|PubMed:21228232, ECO:0000269|PubMed:21266548, ECO:0000305|PubMed:18078692 source Swiss-Prot : SWS_FT_FI2

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