eF-site ID 2fvz-ABCD PDB Code 2fvz Chain A, B, C, D click to enlarge Title Human Inositol Monophosphosphatase 2 Classification HYDROLASE Compound Inositol monophosphatase 2 Source Homo sapiens (Human) (IMPA2_HUMAN) Sequence A:  WEECFQAAVQLALRAGQIIRKALTEETETDHLVEDLIISE LRERFPSHRFIAEEAKCVLTHSPTWIIDPIDGTCNFVHRF PTVAVSIGFAVRQELEFGVIYHCTEERLYTGRRGRGAFCN GQRLRVSGETDLSKALVLTEIGPKRDPATLKLFLSNMERL LHAKAHGVRVIGSSTLALCHLASGAADAYYQFGLHCWDLA AATVIIREAGGIVIDTSGGPLDLMACRVVAASTREMAMLI AQAL B:  WEECFQAAVQLALRAGQIIRKALTEETETDHLVEDLIISE LRERFPSHRFIAEEAKCVLTHSPTWIIDPIDGTCNFVHRF PTVAVSIGFAVRQELEFGVIYHCTEERLYTGRRGRGAFCN GQRLRVSGETDLSKALVLTEIGPKRDPATLKLFLSNMERL LHAKAHGVRVIGSSTLALCHLASGAADAYYQFGLHCWDLA AATVIIREAGGIVIDTSGGPLDLMACRVVAASTREMAMLI AQAL C:  WEECFQAAVQLALRAGQIIRKALTEETETDHLVEDLIISE LRERFPSHRFIAEEAKCVLTHSPTWIIDPIDGTCNFVHRF PTVAVSIGFAVRQELEFGVIYHCTEERLYTGRRGRGAFCN GQRLRVSGETDLSKALVLTEIGPKRDPATLKLFLSNMERL LHAKAHGVRVIGSSTLALCHLASGAADAYYQFGLHCWDLA AATVIIREAGGIVIDTSGGPLDLMACRVVAASTREMAMLI AQAL D:  WEECFQAAVQLALRAGQIIRKALTEETETDHLVEDLIISE LRERFPSHRFIAEEAKCVLTHSPTWIIDPIDGTCNFVHRF PTVAVSIGFAVRQELEFGVIYHCTEERLYTGRRGRGAFCN GQRLRVSGETDLSKALVLTEIGPKRDPATLKLFLSNMERL LHAKAHGVRVIGSSTLALCHLASGAADAYYQFGLHCWDLA AATVIIREAGGIVIDTSGGPLDLMACRVVAASTREMAMLI AQAL Description (1)  Inositol monophosphatase 2 (E.C.3.1.3.25) Functional site 1) chain C residue 231 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 2) chain B residue 231 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 3) chain D residue 231 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 4) chain A residue 231 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 5) chain A residue 98-111 type prosite sequence WIIDPIDGTCNFVH description IMP_1 Inositol monophosphatase family signature 1. WiIDPIDGTcnFvH source prosite : PS00629 6) chain A residue 230-244 type prosite sequence WDLAAATVIIREAGG description IMP_2 Inositol monophosphatase family signature 2. WDlAAAtVIIreaGG source prosite : PS00630 7) chain B residue 224 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:17340635 source Swiss-Prot : SWS_FT_FI1 8) chain C residue 81 type BINDING sequence E description BINDING => ECO:0000269|PubMed:17340635 source Swiss-Prot : SWS_FT_FI1 9) chain C residue 224 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:17340635 source Swiss-Prot : SWS_FT_FI1 10) chain D residue 81 type BINDING sequence E description BINDING => ECO:0000269|PubMed:17340635 source Swiss-Prot : SWS_FT_FI1 11) chain D residue 224 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:17340635 source Swiss-Prot : SWS_FT_FI1 12) chain A residue 81 type BINDING sequence E description BINDING => ECO:0000269|PubMed:17340635 source Swiss-Prot : SWS_FT_FI1 13) chain A residue 224 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:17340635 source Swiss-Prot : SWS_FT_FI1 14) chain B residue 81 type BINDING sequence E description BINDING => ECO:0000269|PubMed:17340635 source Swiss-Prot : SWS_FT_FI1 15) chain A residue 104 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P29218 source Swiss-Prot : SWS_FT_FI2 16) chain B residue 101 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P29218 source Swiss-Prot : SWS_FT_FI2 17) chain B residue 103 type BINDING sequence I description BINDING => ECO:0000250|UniProtKB:P29218 source Swiss-Prot : SWS_FT_FI2 18) chain B residue 104 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P29218 source Swiss-Prot : SWS_FT_FI2 19) chain C residue 101 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P29218 source Swiss-Prot : SWS_FT_FI2 20) chain C residue 103 type BINDING sequence I description BINDING => ECO:0000250|UniProtKB:P29218 source Swiss-Prot : SWS_FT_FI2 21) chain C residue 104 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P29218 source Swiss-Prot : SWS_FT_FI2 22) chain D residue 101 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P29218 source Swiss-Prot : SWS_FT_FI2 23) chain D residue 103 type BINDING sequence I description BINDING => ECO:0000250|UniProtKB:P29218 source Swiss-Prot : SWS_FT_FI2 24) chain D residue 104 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P29218 source Swiss-Prot : SWS_FT_FI2 25) chain A residue 101 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P29218 source Swiss-Prot : SWS_FT_FI2 26) chain A residue 103 type BINDING sequence I description BINDING => ECO:0000250|UniProtKB:P29218 source Swiss-Prot : SWS_FT_FI2 27) chain B residue 205 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI3 28) chain C residue 205 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI3 29) chain D residue 205 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI3 30) chain A residue 205 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI3

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