eF-site ID 4orb-B PDB Code 4orb Chain B click to enlarge Title Crystal structure of mouse calcineurin Classification HYDROLASE/METAL BINDING PROTEIN Compound Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform Source Mus musculus (Mouse) (CANB1_MOUSE) Sequence B:  SYPLEMCSHFDADEIKRLGKRFKKLDLDNSGSLSVEEFMS LPELQQNPLVQRVIDIFDTDGNGEVDFKEFIEGVSQFSVK GDKEQKLRFAFRIYDMDKDGYISNGELFQVLKMMVGNNLK DTQLQQIVDKTIINADKDGDGRISFEEFCAVVGGLDIHKK MVVDV Description Functional site 1) chain B residue 62 type sequence D description BINDING SITE FOR RESIDUE CA B 201 source : AC3 2) chain B residue 64 type sequence D description BINDING SITE FOR RESIDUE CA B 201 source : AC3 3) chain B residue 66 type sequence N description BINDING SITE FOR RESIDUE CA B 201 source : AC3 4) chain B residue 68 type sequence E description BINDING SITE FOR RESIDUE CA B 201 source : AC3 5) chain B residue 73 type sequence E description BINDING SITE FOR RESIDUE CA B 201 source : AC3 6) chain B residue 99 type sequence D description BINDING SITE FOR RESIDUE CA B 202 source : AC4 7) chain B residue 101 type sequence D description BINDING SITE FOR RESIDUE CA B 202 source : AC4 8) chain B residue 103 type sequence D description BINDING SITE FOR RESIDUE CA B 202 source : AC4 9) chain B residue 105 type sequence Y description BINDING SITE FOR RESIDUE CA B 202 source : AC4 10) chain B residue 110 type sequence E description BINDING SITE FOR RESIDUE CA B 202 source : AC4 11) chain B residue 140 type sequence D description BINDING SITE FOR RESIDUE CA B 203 source : AC5 12) chain B residue 142 type sequence D description BINDING SITE FOR RESIDUE CA B 203 source : AC5 13) chain B residue 144 type sequence D description BINDING SITE FOR RESIDUE CA B 203 source : AC5 14) chain B residue 146 type sequence R description BINDING SITE FOR RESIDUE CA B 203 source : AC5 15) chain B residue 151 type sequence E description BINDING SITE FOR RESIDUE CA B 203 source : AC5 16) chain B residue 30 type sequence D description BINDING SITE FOR RESIDUE CA B 204 source : AC6 17) chain B residue 32 type sequence D description BINDING SITE FOR RESIDUE CA B 204 source : AC6 18) chain B residue 34 type sequence S description BINDING SITE FOR RESIDUE CA B 204 source : AC6 19) chain B residue 36 type sequence S description BINDING SITE FOR RESIDUE CA B 204 source : AC6 20) chain B residue 41 type sequence E description BINDING SITE FOR RESIDUE CA B 204 source : AC6 21) chain B residue 30-42 type prosite sequence DLDNSGSLSVEEF description EF_HAND_1 EF-hand calcium-binding domain. DLDNSGSLSveEF source prosite : PS00018 22) chain B residue 62-74 type prosite sequence DTDGNGEVDFKEF description EF_HAND_1 EF-hand calcium-binding domain. DLDNSGSLSveEF source prosite : PS00018 23) chain B residue 99-111 type prosite sequence DMDKDGYISNGEL description EF_HAND_1 EF-hand calcium-binding domain. DLDNSGSLSveEF source prosite : PS00018 24) chain B residue 140-152 type prosite sequence DKDGDGRISFEEF description EF_HAND_1 EF-hand calcium-binding domain. DLDNSGSLSveEF source prosite : PS00018 25) chain B residue 30 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB source Swiss-Prot : SWS_FT_FI1 26) chain B residue 73 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB source Swiss-Prot : SWS_FT_FI1 27) chain B residue 99 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB source Swiss-Prot : SWS_FT_FI1 28) chain B residue 101 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB source Swiss-Prot : SWS_FT_FI1 29) chain B residue 103 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB source Swiss-Prot : SWS_FT_FI1 30) chain B residue 105 type BINDING sequence Y description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB source Swiss-Prot : SWS_FT_FI1 31) chain B residue 110 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB source Swiss-Prot : SWS_FT_FI1 32) chain B residue 140 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB source Swiss-Prot : SWS_FT_FI1 33) chain B residue 142 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB source Swiss-Prot : SWS_FT_FI1 34) chain B residue 144 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB source Swiss-Prot : SWS_FT_FI1 35) chain B residue 146 type BINDING sequence R description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB source Swiss-Prot : SWS_FT_FI1 36) chain B residue 32 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB source Swiss-Prot : SWS_FT_FI1 37) chain B residue 151 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB source Swiss-Prot : SWS_FT_FI1 38) chain B residue 34 type BINDING sequence S description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB source Swiss-Prot : SWS_FT_FI1 39) chain B residue 36 type BINDING sequence S description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB source Swiss-Prot : SWS_FT_FI1 40) chain B residue 41 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB source Swiss-Prot : SWS_FT_FI1 41) chain B residue 62 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB source Swiss-Prot : SWS_FT_FI1 42) chain B residue 64 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB source Swiss-Prot : SWS_FT_FI1 43) chain B residue 66 type BINDING sequence N description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB source Swiss-Prot : SWS_FT_FI1 44) chain B residue 68 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB source Swiss-Prot : SWS_FT_FI1 45) chain B residue 117 type SITE sequence M description Interaction with PxVP motif in substrates of the catalytic subunit => ECO:0000250|UniProtKB:P63098 source Swiss-Prot : SWS_FT_FI2 46) chain B residue 121 type SITE sequence N description Interaction with PxVP motif in substrates of the catalytic subunit => ECO:0000250|UniProtKB:P63098 source Swiss-Prot : SWS_FT_FI2 47) chain B residue 105 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:18034455 source Swiss-Prot : SWS_FT_FI3

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