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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6MNX

Structural basis of impaired hydrolysis in KRAS Q61H mutant

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003924	molecular_function	GTPase activity
A	0005525	molecular_function	GTP binding
A	0007165	biological_process	signal transduction
A	0016020	cellular_component	membrane
B	0003924	molecular_function	GTPase activity
B	0005525	molecular_function	GTP binding
B	0007165	biological_process	signal transduction
B	0016020	cellular_component	membrane
C	0003924	molecular_function	GTPase activity
C	0005525	molecular_function	GTP binding
C	0007165	biological_process	signal transduction
C	0016020	cellular_component	membrane
D	0003924	molecular_function	GTPase activity
D	0005525	molecular_function	GTP binding
D	0007165	biological_process	signal transduction
D	0016020	cellular_component	membrane
E	0003924	molecular_function	GTPase activity
E	0005525	molecular_function	GTP binding
E	0007165	biological_process	signal transduction
E	0016020	cellular_component	membrane
F	0003924	molecular_function	GTPase activity
F	0005525	molecular_function	GTP binding
F	0007165	biological_process	signal transduction
F	0016020	cellular_component	membrane

Functional Information from PDB Data

site_id	AC1
Number of Residues	25
Details	binding site for residue GTP A 201

Chain	Residue
A	GLY13
A	TYR32
A	PRO34
A	THR35
A	GLY60
A	ASN116
A	LYS117
A	ASP119
A	LEU120
A	SER145
A	ALA146
A	VAL14
A	LYS147
A	MG202
A	HOH309
A	HOH319
A	HOH321
A	HOH329
A	GLY15
A	LYS16
A	SER17
A	ALA18
A	PHE28
A	VAL29
A	ASP30

site_id	AC2
Number of Residues	5
Details	binding site for residue MG A 202

Chain	Residue
A	SER17
A	THR35
A	GTP201
A	HOH309
A	HOH319

site_id	AC3
Number of Residues	26
Details	binding site for residue GTP B 201

Chain	Residue
B	GLY12
B	GLY13
B	VAL14
B	GLY15
B	LYS16
B	SER17
B	ALA18
B	PHE28
B	VAL29
B	ASP30
B	TYR32
B	PRO34
B	THR35
B	GLY60
B	ASN116
B	LYS117
B	ASP119
B	LEU120
B	SER145
B	ALA146
B	LYS147
B	MG202
B	HOH307
B	HOH311
B	HOH317
B	HOH324

site_id	AC4
Number of Residues	5
Details	binding site for residue MG B 202

Chain	Residue
B	SER17
B	THR35
B	GTP201
B	HOH307
B	HOH317

site_id	AC5
Number of Residues	29
Details	binding site for residue GTP C 201

Chain	Residue
C	GLY12
C	GLY13
C	VAL14
C	GLY15
C	LYS16
C	SER17
C	ALA18
C	PHE28
C	VAL29
C	ASP30
C	TYR32
C	PRO34
C	THR35
C	GLY60
C	ASN116
C	LYS117
C	ASP119
C	LEU120
C	SER145
C	ALA146
C	LYS147
C	MG202
C	HOH305
C	HOH306
C	HOH310
C	HOH311
C	HOH317
C	HOH319
C	HOH323

site_id	AC6
Number of Residues	5
Details	binding site for residue MG C 202

Chain	Residue
C	SER17
C	THR35
C	GTP201
C	HOH306
C	HOH317

site_id	AC7
Number of Residues	28
Details	binding site for residue GTP D 201

Chain	Residue
D	SER17
D	ALA18
D	PHE28
D	VAL29
D	ASP30
D	TYR32
D	PRO34
D	THR35
D	GLY60
D	ASN116
D	LYS117
D	ASP119
D	LEU120
D	SER145
D	ALA146
D	LYS147
D	MG202
D	HOH307
D	HOH310
D	HOH312
D	HOH314
D	HOH319
D	HOH321
D	HOH327
D	GLY13
D	VAL14
D	GLY15
D	LYS16

site_id	AC8
Number of Residues	5
Details	binding site for residue MG D 202

Chain	Residue
D	SER17
D	THR35
D	GTP201
D	HOH307
D	HOH312

site_id	AC9
Number of Residues	26
Details	binding site for residue GTP E 201

Chain	Residue
E	GLY12
E	GLY13
E	VAL14
E	GLY15
E	LYS16
E	SER17
E	ALA18
E	PHE28
E	VAL29
E	ASP30
E	TYR32
E	PRO34
E	THR35
E	GLY60
E	ASN116
E	LYS117
E	ASP119
E	LEU120
E	SER145
E	ALA146
E	LYS147
E	MG202
E	HOH302
E	HOH316
E	HOH317
E	HOH320

site_id	AD1
Number of Residues	5
Details	binding site for residue MG E 202

Chain	Residue
E	SER17
E	THR35
E	GTP201
E	HOH302
E	HOH317

site_id	AD2
Number of Residues	23
Details	binding site for residue GTP F 201

Chain	Residue
F	GLY13
F	VAL14
F	GLY15
F	LYS16
F	SER17
F	ALA18
F	PHE28
F	VAL29
F	ASP30
F	TYR32
F	PRO34
F	THR35
F	GLY60
F	ASN116
F	LYS117
F	ASP119
F	LEU120
F	SER145
F	ALA146
F	LYS147
F	MG202
F	HOH301
F	HOH306

site_id	AD3
Number of Residues	5
Details	binding site for residue MG F 202

Chain	Residue
F	SER17
F	THR35
F	GTP201
F	HOH301
F	HOH302

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	BINDING: BINDING => ECO:0000269\|PubMed:22431598, ECO:0000269\|PubMed:22566140

Chain	Residue	Details
A	GLY10
C	VAL29
C	ALA59
C	ASN116
D	GLY10
D	VAL29
D	ALA59
D	ASN116
E	GLY10
E	VAL29
E	ALA59
A	VAL29
E	ASN116
F	GLY10
F	VAL29
F	ALA59
F	ASN116
A	ALA59
A	ASN116
B	GLY10
B	VAL29
B	ALA59
B	ASN116
C	GLY10

site_id	SWS_FT_FI2
Number of Residues	6
Details	MOD_RES: N-acetylmethionine; in GTPase KRas; alternate => ECO:0000269\|Ref.17

Chain	Residue	Details
A	MET1
B	MET1
C	MET1
D	MET1
E	MET1
F	MET1

site_id	SWS_FT_FI3
Number of Residues	6
Details	MOD_RES: N-acetylthreonine; in GTPase KRas, N-terminally processed => ECO:0000269\|Ref.17

Chain	Residue	Details
A	THR2
B	THR2
C	THR2
D	THR2
E	THR2
F	THR2

site_id	SWS_FT_FI4
Number of Residues	6
Details	MOD_RES: N6-acetyllysine => ECO:0000269\|PubMed:22711838

Chain	Residue	Details
A	LYS104
B	LYS104
C	LYS104
D	LYS104
E	LYS104
F	LYS104

site_id	SWS_FT_FI5
Number of Residues	6
Details	CARBOHYD: (Microbial infection) O-linked (Glc) threonine; by P.sordellii toxin TcsL => ECO:0000269\|PubMed:19744486

Chain	Residue	Details
A	THR35
B	THR35
C	THR35
D	THR35
E	THR35
F	THR35

224004

PDB entries from 2024-08-21

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