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3H4S

Structure of the complex of a mitotic kinesin with its calcium binding regulator

Functional Information from GO Data
ChainGOidnamespacecontents
A0003777molecular_functionmicrotubule motor activity
A0005524molecular_functionATP binding
A0007018biological_processmicrotubule-based movement
A0008017molecular_functionmicrotubule binding
E0005509molecular_functioncalcium ion binding
E0005515molecular_functionprotein binding
E0010091biological_processtrichome branching
E0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE ADP A 600
ChainResidue
AHOH8
APRO898
AGLN971
AGLY973
ASER974
AGLY975
ALYS976
ATHR977
APHE978
AHOH25
AHOH84
AHOH85
AHOH89
AHOH93
AHOH99
AMG601
AARG897

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 601
ChainResidue
AHOH84
AHOH85
AHOH86
AHOH87
AADP600
ATHR977

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 602
ChainResidue
AVAL964
ALYS1111
ASER1113
ASER1174

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA E 700
ChainResidue
EASP87
EASP89
EASP91
EALA93
EGLU98
EHOH147

Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DLDGDGALNqtEF
ChainResidueDetails
EASP87-PHE99

site_idPS00411
Number of Residues12
DetailsKINESIN_MOTOR_1 Kinesin motor domain signature. GKLsFVDLAGSE
ChainResidueDetails
AGLY1110-GLU1121

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448
ChainResidueDetails
EASP87
EASP89
EASP91
EGLU98

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1goj
ChainResidueDetails
AGLY1119

223532

PDB entries from 2024-08-07

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