Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5USJ

Crystal Structure of human KRAS G12D mutant in complex with GDPNP

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	5
Details	binding site for residue MG A 1001

Chain	Residue
A	SER17
A	THR35
A	GNP1002
A	HOH1104
A	HOH1131

site_id	AC2
Number of Residues	28
Details	binding site for residue GNP A 1002

Chain	Residue
A	LYS16
A	SER17
A	ALA18
A	PHE28
A	VAL29
A	ASP30
A	TYR32
A	PRO34
A	THR35
A	GLY60
A	ASN116
A	LYS117
A	ASP119
A	LEU120
A	SER145
A	ALA146
A	LYS147
A	MG1001
A	HOH1104
A	HOH1131
A	HOH1140
A	HOH1142
A	HOH1147
A	HOH1203
A	ASP12
A	GLY13
A	VAL14
A	GLY15

site_id	AC3
Number of Residues	5
Details	binding site for residue MG B 1001

Chain	Residue
B	SER17
B	THR35
B	GNP1002
B	HOH1117
B	HOH1121

site_id	AC4
Number of Residues	27
Details	binding site for residue GNP B 1002

Chain	Residue
B	ASP12
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	MG1001
B	HOH1110
B	HOH1117
B	HOH1121
B	HOH1172
B	HOH1179

site_id	AC5
Number of Residues	5
Details	binding site for residue MG C 1001

Chain	Residue
C	SER17
C	THR35
C	GNP1002
C	HOH1103
C	HOH1123

site_id	AC6
Number of Residues	26
Details	binding site for residue GNP C 1002

Chain	Residue
C	ASP12
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	MG1001
C	HOH1103
C	HOH1123
C	HOH1140
C	HOH1166

site_id	AC7
Number of Residues	5
Details	binding site for residue MG D 1001

Chain	Residue
D	HOH1137
D	HOH1138
D	SER17
D	THR35
D	GNP1002

site_id	AC8
Number of Residues	29
Details	binding site for residue GNP D 1002

Chain	Residue
D	ASP12
D	GLY13
D	VAL14
D	GLY15
D	LYS16
D	SER17
D	ALA18
D	PHE28
D	VAL29
D	ASP30
D	GLU31
D	TYR32
D	PRO34
D	THR35
D	GLY60
D	ASN116
D	LYS117
D	ASP119
D	LEU120
D	SER145
D	ALA146
D	LYS147
D	MG1001
D	HOH1129
D	HOH1133
D	HOH1137
D	HOH1138
D	HOH1149
D	HOH1183

site_id	AC9
Number of Residues	5
Details	binding site for residue MG E 1001

Chain	Residue
E	SER17
E	THR35
E	GNP1002
E	HOH1111
E	HOH1123

site_id	AD1
Number of Residues	30
Details	binding site for residue GNP E 1002

Chain	Residue
E	ASP12
E	GLY13
E	VAL14
E	GLY15
E	LYS16
E	SER17
E	ALA18
E	PHE28
E	VAL29
E	ASP30
E	GLU31
E	PRO34
E	THR35
E	GLY60
E	ASN116
E	LYS117
E	ASP119
E	LEU120
E	SER145
E	ALA146
E	LYS147
E	MG1001
E	HOH1111
E	HOH1123
E	HOH1125
E	HOH1138
E	HOH1151
E	HOH1167
E	HOH1170
E	HOH1180

site_id	AD2
Number of Residues	5
Details	binding site for residue MG F 1001

Chain	Residue
F	SER17
F	THR35
F	GNP1002
F	HOH1110
F	HOH1118

site_id	AD3
Number of Residues	27
Details	binding site for residue GNP F 1002

Chain	Residue
F	ASP12
F	GLY13
F	VAL14
F	GLY15
F	LYS16
F	SER17
F	ALA18
F	PHE28
F	VAL29
F	ASP30
F	PRO34
F	THR35
F	GLY60
F	ASN116
F	LYS117
F	ASP119
F	LEU120
F	SER145
F	ALA146
F	LYS147
F	MG1001
F	HOH1110
F	HOH1118
F	HOH1126
F	HOH1151
F	HOH1157
F	HOH1174

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	48
Details	Motif: {"description":"Effector region"}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	108
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22431598","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22566140","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"34380736","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"35522713","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	6
Details	Modified residue: {"description":"N-acetylmethionine; in GTPase KRas; alternate","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2008","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Calvo F.","Kolch W."]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	6
Details	Modified residue: {"description":"N-acetylthreonine; in GTPase KRas, N-terminally processed","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2008","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Calvo F.","Kolch W."]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	6
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"22711838","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	6
Details	Glycosylation: {"description":"(Microbial infection) O-linked (Glc) threonine; by P.sordellii toxin TcsL","evidences":[{"source":"PubMed","id":"19744486","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)