5HNW

Structural basis of backwards motion in kinesin-14: minus-end directed nKn664 in the AMPPNP state

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000226	biological_process	microtubule cytoskeleton organization
A	0000278	biological_process	mitotic cell cycle
A	0003924	molecular_function	GTPase activity
A	0005200	molecular_function	structural constituent of cytoskeleton
A	0005525	molecular_function	GTP binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005856	cellular_component	cytoskeleton
A	0005874	cellular_component	microtubule
A	0007017	biological_process	microtubule-based process
A	0015630	cellular_component	microtubule cytoskeleton
A	0016787	molecular_function	hydrolase activity
A	0046872	molecular_function	metal ion binding
B	0000226	biological_process	microtubule cytoskeleton organization
B	0000278	biological_process	mitotic cell cycle
B	0003924	molecular_function	GTPase activity
B	0005200	molecular_function	structural constituent of cytoskeleton
B	0005525	molecular_function	GTP binding
B	0005737	cellular_component	cytoplasm
B	0005856	cellular_component	cytoskeleton
B	0005874	cellular_component	microtubule
B	0007017	biological_process	microtubule-based process
B	0007399	biological_process	nervous system development
B	0015630	cellular_component	microtubule cytoskeleton
B	0046872	molecular_function	metal ion binding
B	0046982	molecular_function	protein heterodimerization activity
B	1902669	biological_process	positive regulation of axon guidance
K	0003777	molecular_function	microtubule motor activity
K	0005524	molecular_function	ATP binding
K	0007018	biological_process	microtubule-based movement
K	0008017	molecular_function	microtubule binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue MG A 501

Chain	Residue
A	GLN11
A	ASP69
A	GLU71
A	VAL74
A	GTP502

---

site_id	AC2
Number of Residues	17
Details	binding site for residue GTP A 502

Chain	Residue
A	ALA99
A	ASN101
A	SER140
A	GLY144
A	THR145
A	ILE171
A	ASN206
A	TYR224
A	LEU227
A	ASN228
A	MG501
B	LEU248
B	LYS254
A	GLY10
A	GLN11
A	ALA12
A	GLN15

---

site_id	AC3
Number of Residues	13
Details	binding site for residue GDP B 901

Chain	Residue
B	GLN11
B	CYS12
B	GLN15
B	SER140
B	GLY142
B	GLY143
B	GLY144
B	THR145
B	GLY146
B	ASP179
B	ASN206
B	TYR224
B	ASN228

---

site_id	AC4
Number of Residues	17
Details	binding site for residue TA1 B 902

Chain	Residue
B	GLU22
B	VAL23
B	ASP26
B	GLU27
B	ASP226
B	HIS229
B	LEU230
B	ALA233
B	SER236
B	PHE272
B	PRO274
B	LEU275
B	THR276
B	ARG278
B	PRO360
B	ARG369
B	GLY370

---

site_id	AC5
Number of Residues	3
Details	binding site for residue MG K 401

Chain	Residue
K	THR108
K	HIS216
K	ANP402

---

site_id	AC6
Number of Residues	12
Details	binding site for residue ANP K 402

Chain	Residue
K	ARG30
K	GLN102
K	THR103
K	SER104
K	SER105
K	GLY106
K	LYS107
K	THR108
K	HIS109
K	ASN214
K	HIS216
K	MG401

---

Functional Information from PROSITE/UniProt

site_id	PS00227
Number of Residues	7
Details	TUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG

Chain	Residue	Details
A	GLY142-GLY148
B	GLY142-GLY148

---

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

Chain	Residue	Details
K	GLY241-GLU252

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|PubMed:27452403, ECO:0007744|PDB:5HLE

Chain	Residue	Details
K	THR103
K	SER105
K	GLY106
K	LYS107
K	THR108
K	HIS109
K	THR110
K	LEU115

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P68363

Chain	Residue	Details
B	GLU71
A	GLU71
A	SER140
A	GLY144
A	THR145
A	THR179
A	ASN206
A	ASN228

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P99024

Chain	Residue	Details
B	SER40

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q3KRE8

Chain	Residue	Details
B	ALA57

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024

Chain	Residue	Details
B	LYS60
A	GLY232

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q9BVA1

Chain	Residue	Details
B	SER174

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P07437

Chain	Residue	Details
B	THR287
B	THR292

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437

Chain	Residue	Details
B	ARG320

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	MOD_RES: 5-glutamyl polyglutamate => ECO:0000250|UniProtKB:Q2T9S0

Chain	Residue	Details
B	GLU448

---

site_id	SWS_FT_FI10
Number of Residues	1
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P07437

Chain	Residue	Details
B	LYS60

---

site_id	SWS_FT_FI11
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P07437

Chain	Residue	Details
A	TYR451
B	LYS326

---

site_id	SWS_FT_FI12
Number of Residues	3
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P68363

Chain	Residue	Details
A	LYS326
A	LYS370

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