1VFZ

Crystal Structure of the Kif1A Motor Domain Complexed With ADP-Mg-VO4

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	8
Details	BINDING SITE FOR RESIDUE VO4 A 400

Chain	Residue
A	GLN72
A	MET210
A	GLU212
A	ARG216
A	GLY262
A	HOH581
A	HOH613
A	HOH625

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 501

Chain	Residue
A	ADP500
A	HOH502
A	HOH594
A	HOH595
A	HOH596
A	SER104

---

site_id	AC3
Number of Residues	22
Details	BINDING SITE FOR RESIDUE ADP A 500

Chain	Residue
A	ARG11
A	ARG13
A	SER58
A	GLU63
A	ASP64
A	ILE65
A	TYR67
A	THR99
A	GLY100
A	ALA101
A	GLY102
A	LYS103
A	SER104
A	TYR105
A	MG501
A	HOH502
A	HOH549
A	HOH583
A	HOH589
A	HOH594
A	HOH596
A	HOH645

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	SER242-GLU253

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:18806800, ECO:0000269|PubMed:35132656, ECO:0000305|PubMed:15286375, ECO:0007744|PDB:1VFX, ECO:0007744|PDB:1VFZ, ECO:0007744|PDB:2ZFI, ECO:0007744|PDB:2ZFJ, ECO:0007744|PDB:2ZFK, ECO:0007744|PDB:2ZFL, ECO:0007744|PDB:2ZFM, ECO:0007744|PDB:7EO9, ECO:0007744|PDB:7EOB

Chain	Residue	Details
A	TYR67

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:18806800, ECO:0000269|PubMed:35132656, ECO:0000305|PubMed:15286375, ECO:0007744|PDB:1VFX, ECO:0007744|PDB:1VFZ, ECO:0007744|PDB:2ZFI, ECO:0007744|PDB:2ZFK, ECO:0007744|PDB:2ZFL, ECO:0007744|PDB:2ZFM, ECO:0007744|PDB:7EO9, ECO:0007744|PDB:7EOB

Chain	Residue	Details
A	GLY100

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:18806800, ECO:0000269|PubMed:35132656, ECO:0000305|PubMed:15286375, ECO:0007744|PDB:1VFX, ECO:0007744|PDB:2ZFJ, ECO:0007744|PDB:2ZFK, ECO:0007744|PDB:2ZFL, ECO:0007744|PDB:2ZFM, ECO:0007744|PDB:7EO9

Chain	Residue	Details
A	ALA101

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000305|PubMed:15286375, ECO:0007744|PDB:1VFV, ECO:0007744|PDB:1VFW

Chain	Residue	Details
A	GLY102
A	LYS103
A	TYR105
A	SER215

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:15286375, ECO:0000269|PubMed:18806800, ECO:0000269|PubMed:35132656, ECO:0007744|PDB:1VFV, ECO:0007744|PDB:1VFW, ECO:0007744|PDB:1VFX, ECO:0007744|PDB:1VFZ, ECO:0007744|PDB:2ZFI, ECO:0007744|PDB:2ZFK, ECO:0007744|PDB:7EO9, ECO:0007744|PDB:7EOB

Chain	Residue	Details
A	SER104

---

Catalytic Information from CSA

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

Chain	Residue	Details
A	GLY251

---