eF-site ID 2hhl-ABC PDB Code 2hhl Chain A, B, C click to enlarge Title Crystal structure of the human small CTD phosphatase 3 isoform 1 Classification HYDROLASE Compound CTD small phosphatase-like protein Source (CTDSL_HUMAN) Sequence A:  QVIPIPSPPAKYLLPEVTVLDYGKKCVVIDLDETLVHSSF KPISNADFIVPVEIDGTIHQVYVLKRPHVDEFLQRMGQLF ECVLFTASLAKYADPVADLLDRWGVFRARLFRESCVFHRG NYVKDLSRLGRELSKVIIVDNSPASYIFHPENAVPVQSWF DDMTDTELLDLIPFFEGLSR B:  VIPIPSPPAKYLLPEVTVLDYGKKCVVIDLDETLVHSSFK PISNADFIVPVEIDGTIHQVYVLKRPHVDEFLQRMGQLFE CVLFTASLAKYADPVADLLDRWGVFRARLFRESCVFHRGN YVKDLSRLGRELSKVIIVDNSPASYIFHPENAVPVQSWFD DMTDTELLDLIPFFEGLSR C:  LRQVIPIPSPPAKYLLPEVTVLDYGKKCVVIDLDETLVHS SFKPISNADFIVPVEIDGTIHQVYVLKRPHVDEFLQRMGQ LFECVLFTASLAKYADPVADLLDRWGVFRARLFRESCVFH RGNYVKDLSRLGRELSKVIIVDNSPASYIFHPENAVPVQS WFDDMTDTELLDLIPFFEGLSRED Description Functional site 1) chain A residue 26 type sequence Y description BINDING SITE FOR RESIDUE KEG A 902 source : AC1 2) chain A residue 27 type sequence G description BINDING SITE FOR RESIDUE KEG A 902 source : AC1 3) chain A residue 28 type sequence K description BINDING SITE FOR RESIDUE KEG A 902 source : AC1 4) chain A residue 41 type sequence H description BINDING SITE FOR RESIDUE KEG A 902 source : AC1 5) chain A residue 43 type sequence S description BINDING SITE FOR RESIDUE KEG A 902 source : AC1 6) chain A residue 44 type sequence F description BINDING SITE FOR RESIDUE KEG A 902 source : AC1 7) chain A residue 45 type sequence K description BINDING SITE FOR RESIDUE KEG A 902 source : AC1 8) chain B residue 6 type sequence V description BINDING SITE FOR RESIDUE KEG A 902 source : AC1 9) chain B residue 12 type sequence P description BINDING SITE FOR RESIDUE KEG A 902 source : AC1 10) chain A residue 55 type sequence P description BINDING SITE FOR RESIDUE KEG C 900 source : AC2 11) chain A residue 62 type sequence I description BINDING SITE FOR RESIDUE KEG C 900 source : AC2 12) chain A residue 64 type sequence Q description BINDING SITE FOR RESIDUE KEG C 900 source : AC2 13) chain C residue 43 type sequence S description BINDING SITE FOR RESIDUE KEG C 900 source : AC2 14) chain C residue 44 type sequence F description BINDING SITE FOR RESIDUE KEG C 900 source : AC2 15) chain C residue 45 type sequence K description BINDING SITE FOR RESIDUE KEG C 900 source : AC2 16) chain B residue 55 type sequence P description BINDING SITE FOR RESIDUE KEG D 901 source : AC3 17) chain B residue 62 type sequence I description BINDING SITE FOR RESIDUE KEG D 901 source : AC3 18) chain B residue 64 type sequence Q description BINDING SITE FOR RESIDUE KEG D 901 source : AC3 19) chain A residue 34 type ACT_SITE sequence D description 4-aspartylphosphate intermediate => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 20) chain B residue 34 type ACT_SITE sequence D description 4-aspartylphosphate intermediate => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 21) chain C residue 34 type ACT_SITE sequence D description 4-aspartylphosphate intermediate => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 22) chain A residue 36 type ACT_SITE sequence D description Proton donor => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 23) chain B residue 36 type ACT_SITE sequence D description Proton donor => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 24) chain C residue 36 type ACT_SITE sequence D description Proton donor => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 25) chain A residue 34 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 26) chain A residue 36 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 27) chain A residue 145 type BINDING sequence N description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 28) chain B residue 34 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 29) chain B residue 36 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 30) chain B residue 145 type BINDING sequence N description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 31) chain C residue 34 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 32) chain C residue 36 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 33) chain C residue 145 type BINDING sequence N description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 34) chain A residue 90 type SITE sequence T description Transition state stabilizer => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 35) chain A residue 128 type SITE sequence K description Transition state stabilizer => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 36) chain B residue 90 type SITE sequence T description Transition state stabilizer => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 37) chain B residue 128 type SITE sequence K description Transition state stabilizer => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 38) chain C residue 90 type SITE sequence T description Transition state stabilizer => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 39) chain C residue 128 type SITE sequence K description Transition state stabilizer => ECO:0000250 source Swiss-Prot : SWS_FT_FI4

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