eF-site ID 3kin-ABCD PDB Code 3kin Chain A, B, C, D click to enlarge Title KINESIN (DIMERIC) FROM RATTUS NORVEGICUS Classification MOTOR PROTEIN Compound KINESIN HEAVY CHAIN Source (3KIN) Sequence A:  ADPAECSIKVMCRFRPLNEAEILRGDKFIPKFKGEETVVI GQGKPYVFDRVLPPNTTQEQVYNACAKQIVKDVLEGYNGT IFAYGQTSSGKTHTMEGKLHDPQLMGIIPRIAHDIFDHIY SMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLAVHEDKN RVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEH SSRSHSIFLINIKQENVETEKKLSGKLYLVDLAGSEKV B:  NKSLSALGNVISALAEGTKTHVPYRDSKMTRILQDSLGGN CRTTIVICCSPSVFNEAETKSTLMFGQRAKTIKNTVSVNL ELTAEEWKKKYEKEKEKNKALKSVIQHLEVELNRWRN C:  ADPAECSIKVMCRFRPLNEAEILRGDKFIPKFKGEETVVI GQGKPYVFDRVLPPNTTQEQVYNACAKQIVKDVLEGYNGT IFAYGQTSSGKTHTMEGKLHDPQLMGIIPRIAHDIFDHIY SMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLAVHEDKN RVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEH SSRSHSIFLINIKQENVETEKKLSGKLYLVDLAGSEKV D:  NKSLSALGNVISALAEGTKTHVPYRDSKMTRILQDSLGGN CRTTIVICCSPSVFNEAETKSTLMFGQRAKTIKNTVSVNL ELTAEEWKKKYEKEKEKNKALKSVIQHLEVELNRW Description (1)  KINESIN HEAVY CHAIN, ADENOSINE-5'-DIPHOSPHATE Functional site 1) chain A residue 21 type sequence A description BINDING SITE FOR RESIDUE ADP C 400 source : AC1 2) chain A residue 24 type sequence L description BINDING SITE FOR RESIDUE ADP C 400 source : AC1 3) chain C residue 17 type sequence P description BINDING SITE FOR RESIDUE ADP C 400 source : AC1 4) chain C residue 88 type sequence T description BINDING SITE FOR RESIDUE ADP C 400 source : AC1 5) chain C residue 89 type sequence S description BINDING SITE FOR RESIDUE ADP C 400 source : AC1 6) chain C residue 90 type sequence S description BINDING SITE FOR RESIDUE ADP C 400 source : AC1 7) chain C residue 91 type sequence G description BINDING SITE FOR RESIDUE ADP C 400 source : AC1 8) chain C residue 92 type sequence K description BINDING SITE FOR RESIDUE ADP C 400 source : AC1 9) chain C residue 93 type sequence T description BINDING SITE FOR RESIDUE ADP C 400 source : AC1 10) chain C residue 94 type sequence H description BINDING SITE FOR RESIDUE ADP C 400 source : AC1 11) chain A residue 16 type sequence R description BINDING SITE FOR RESIDUE ADP A 401 source : AC2 12) chain A residue 17 type sequence P description BINDING SITE FOR RESIDUE ADP A 401 source : AC2 13) chain A residue 87 type sequence Q description BINDING SITE FOR RESIDUE ADP A 401 source : AC2 14) chain A residue 89 type sequence S description BINDING SITE FOR RESIDUE ADP A 401 source : AC2 15) chain A residue 90 type sequence S description BINDING SITE FOR RESIDUE ADP A 401 source : AC2 16) chain A residue 91 type sequence G description BINDING SITE FOR RESIDUE ADP A 401 source : AC2 17) chain A residue 92 type sequence K description BINDING SITE FOR RESIDUE ADP A 401 source : AC2 18) chain A residue 93 type sequence T description BINDING SITE FOR RESIDUE ADP A 401 source : AC2 19) chain A residue 94 type sequence H description BINDING SITE FOR RESIDUE ADP A 401 source : AC2 20) chain A residue 124 type sequence D description BINDING SITE FOR RESIDUE ADP A 401 source : AC2 21) chain A residue 125 type sequence E description BINDING SITE FOR RESIDUE ADP A 401 source : AC2 22) chain A residue 87 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:27452403, ECO:0007744|PDB:5HLE source Swiss-Prot : SWS_FT_FI1 23) chain C residue 89 type BINDING sequence S description BINDING => ECO:0000269|PubMed:27452403, ECO:0007744|PDB:5HLE source Swiss-Prot : SWS_FT_FI1 24) chain C residue 90 type BINDING sequence S description BINDING => ECO:0000269|PubMed:27452403, ECO:0007744|PDB:5HLE source Swiss-Prot : SWS_FT_FI1 25) chain C residue 91 type BINDING sequence G description BINDING => ECO:0000269|PubMed:27452403, ECO:0007744|PDB:5HLE source Swiss-Prot : SWS_FT_FI1 26) chain C residue 92 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27452403, ECO:0007744|PDB:5HLE source Swiss-Prot : SWS_FT_FI1 27) chain C residue 93 type BINDING sequence T description BINDING => ECO:0000269|PubMed:27452403, ECO:0007744|PDB:5HLE source Swiss-Prot : SWS_FT_FI1 28) chain C residue 94 type BINDING sequence H description BINDING => ECO:0000269|PubMed:27452403, ECO:0007744|PDB:5HLE source Swiss-Prot : SWS_FT_FI1 29) chain C residue 99 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27452403, ECO:0007744|PDB:5HLE source Swiss-Prot : SWS_FT_FI1 30) chain A residue 89 type BINDING sequence S description BINDING => ECO:0000269|PubMed:27452403, ECO:0007744|PDB:5HLE source Swiss-Prot : SWS_FT_FI1 31) chain A residue 90 type BINDING sequence S description BINDING => ECO:0000269|PubMed:27452403, ECO:0007744|PDB:5HLE source Swiss-Prot : SWS_FT_FI1 32) chain A residue 91 type BINDING sequence G description BINDING => ECO:0000269|PubMed:27452403, ECO:0007744|PDB:5HLE source Swiss-Prot : SWS_FT_FI1 33) chain A residue 92 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27452403, ECO:0007744|PDB:5HLE source Swiss-Prot : SWS_FT_FI1 34) chain A residue 93 type BINDING sequence T description BINDING => ECO:0000269|PubMed:27452403, ECO:0007744|PDB:5HLE source Swiss-Prot : SWS_FT_FI1 35) chain A residue 94 type BINDING sequence H description BINDING => ECO:0000269|PubMed:27452403, ECO:0007744|PDB:5HLE source Swiss-Prot : SWS_FT_FI1 36) chain A residue 99 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27452403, ECO:0007744|PDB:5HLE source Swiss-Prot : SWS_FT_FI1 37) chain C residue 87 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:27452403, ECO:0007744|PDB:5HLE source Swiss-Prot : SWS_FT_FI1 38) chain A residue 226-237 type prosite sequence GKLYLVDLAGSE description KINESIN_MOTOR_1 Kinesin motor domain signature. GKLyLVDLAGSE source prosite : PS00411

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