eF-site ID 2ght-ABCD PDB Code 2ght Chain A, B, C, D click to enlarge Title CTD-specific phosphatase Scp1 in complex with peptide from C-terminal domain of RNA polymerase II Classification HYDROLASE Compound Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 1 Source Homo sapiens (Human) (RPB1_HUMAN) Sequence A:  QYLLPEAKAQDSDKICVVINLDETLVHSSFKPVNNADFII PVEIDGVVHQVYVLKRPHVDEFLQRMGELFECVLFTASLA KYADPVADLLDKWGAFRARLFRESCVFHRGNYVKDLSRLG RDLRRVLILDNSPASYVFHPDNAVPVASWFDNMSDTELHD LLPFFEQLSRVDDVYSVLRQ B:  QYLLPEAKAQDSDKICVVINLDETLVHSSFKPVNNADFII PVEIDGVVHQVYVLKRPHVDEFLQRMGELFECVLFTASLA KYADPVADLLDKWGAFRARLFRESCVFHRGNYVKDLSRLG RDLRRVLILDNSPASYVFHPDNAVPVASWFDNMSDTELHD LLPFFEQLSRVDDVYSVLRQ C:  SPTXP D:  SYSPTXPS Description Functional site 1) chain B residue 96 type sequence N description BINDING SITE FOR RESIDUE MG B 257 source : AC1 2) chain B residue 98 type sequence D description BINDING SITE FOR RESIDUE MG B 257 source : AC1 3) chain B residue 207 type sequence N description BINDING SITE FOR RESIDUE MG B 257 source : AC1 4) chain D residue 174 type sequence X description BINDING SITE FOR RESIDUE MG B 257 source : AC1 5) chain A residue 96 type sequence N description BINDING SITE FOR RESIDUE MG A 257 source : AC2 6) chain A residue 98 type sequence D description BINDING SITE FOR RESIDUE MG A 257 source : AC2 7) chain A residue 207 type sequence N description BINDING SITE FOR RESIDUE MG A 257 source : AC2 8) chain C residue 174 type sequence X description BINDING SITE FOR RESIDUE MG A 257 source : AC2 9) chain A residue 96 type ACT_SITE sequence N description 4-aspartylphosphate intermediate => ECO:0000269|PubMed:15304220, ECO:0000269|PubMed:17157258 source Swiss-Prot : SWS_FT_FI1 10) chain B residue 96 type ACT_SITE sequence N description 4-aspartylphosphate intermediate => ECO:0000269|PubMed:15304220, ECO:0000269|PubMed:17157258 source Swiss-Prot : SWS_FT_FI1 11) chain A residue 98 type ACT_SITE sequence D description Proton donor => ECO:0000305|PubMed:15304220 source Swiss-Prot : SWS_FT_FI2 12) chain B residue 98 type ACT_SITE sequence D description Proton donor => ECO:0000305|PubMed:15304220 source Swiss-Prot : SWS_FT_FI2 13) chain A residue 96 type BINDING sequence N description BINDING => ECO:0000269|PubMed:15304220 source Swiss-Prot : SWS_FT_FI3 14) chain A residue 98 type BINDING sequence D description BINDING => ECO:0000269|PubMed:15304220 source Swiss-Prot : SWS_FT_FI3 15) chain A residue 207 type BINDING sequence N description BINDING => ECO:0000269|PubMed:15304220 source Swiss-Prot : SWS_FT_FI3 16) chain B residue 96 type BINDING sequence N description BINDING => ECO:0000269|PubMed:15304220 source Swiss-Prot : SWS_FT_FI3 17) chain B residue 98 type BINDING sequence D description BINDING => ECO:0000269|PubMed:15304220 source Swiss-Prot : SWS_FT_FI3 18) chain B residue 207 type BINDING sequence N description BINDING => ECO:0000269|PubMed:15304220 source Swiss-Prot : SWS_FT_FI3 19) chain A residue 152 type SITE sequence T description Transition state stabilizer => ECO:0000305|PubMed:15304220 source Swiss-Prot : SWS_FT_FI4 20) chain A residue 190 type SITE sequence K description Transition state stabilizer => ECO:0000305|PubMed:15304220 source Swiss-Prot : SWS_FT_FI4 21) chain B residue 152 type SITE sequence T description Transition state stabilizer => ECO:0000305|PubMed:15304220 source Swiss-Prot : SWS_FT_FI4 22) chain B residue 190 type SITE sequence K description Transition state stabilizer => ECO:0000305|PubMed:15304220 source Swiss-Prot : SWS_FT_FI4

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