1F9U

CRYSTAL STRUCTURES OF MUTANTS REVEAL A SIGNALLING PATHWAY FOR ACTIVATION OF THE KINESIN MOTOR ATPASE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003777	molecular_function	microtubule motor activity
A	0005524	molecular_function	ATP binding
A	0007018	biological_process	microtubule-based movement
A	0008017	molecular_function	microtubule binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 997

Chain	Residue
A	HOH4
A	HOH9
A	HOH89
A	HOH138
A	THR481
A	ADP999

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site_id	AC2
Number of Residues	21
Details	BINDING SITE FOR RESIDUE ADP A 999

Chain	Residue
A	HOH89
A	HOH124
A	HOH129
A	HOH138
A	HOH145
A	ARG392
A	ARG394
A	PRO395
A	GLN475
A	THR476
A	GLY477
A	SER478
A	GLY479
A	LYS480
A	THR481
A	PHE482
A	THR587
A	MG997
A	HOH69
A	HOH79
A	HOH88

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Functional Information from PROSITE/UniProt

site_id	PS00411
Number of Residues	12
Details	KINESIN_MOTOR_1 Kinesin motor domain signature. GTLnLVDLAGSE

Chain	Residue	Details
A	GLY620-GLU631

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	5
Details	BINDING: BINDING => ECO:0000269|PubMed:11387196, ECO:0007744|PDB:1F9V

Chain	Residue	Details
A	ASN386
A	ARG388
A	GLU454
A	LYS579
A	THR694

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site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:11387196, ECO:0000269|PubMed:22734002, ECO:0000269|PubMed:9485302, ECO:0007744|PDB:1F9T, ECO:0007744|PDB:1F9U, ECO:0007744|PDB:1F9V, ECO:0007744|PDB:1F9W, ECO:0007744|PDB:3KAR, ECO:0007744|PDB:4ETP

Chain	Residue	Details
A	ARG392
A	GLY477
A	GLY479
A	LYS480
A	THR481
A	PHE482

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site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:11387196, ECO:0007744|PDB:1F9W

Chain	Residue	Details
A	SER478

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site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:22734002, ECO:0007744|PDB:4ETP

Chain	Residue	Details
A	GLU554

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1goj

Chain	Residue	Details
A	GLY629

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