6O46

Crystal structure of human KRAS P34R mutant in complex with GNP and Phosphate

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	31
Details	binding site for residue GNP A 201

Chain	Residue
A	GLY12
A	ASP30
A	GLY60
A	GLN61
A	ASN116
A	LYS117
A	ASP119
A	LEU120
A	LYS128
A	SER145
A	ALA146
A	GLY13
A	LYS147
A	MG202
A	PO4203
A	HOH301
A	HOH311
A	HOH330
A	HOH356
A	HOH360
A	HOH385
A	HOH407
A	VAL14
A	HOH411
A	HOH412
A	GLY15
A	LYS16
A	SER17
A	ALA18
A	PHE28
A	VAL29

---

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

Chain	Residue
A	SER17
A	GNP201
A	HOH330
A	HOH360
A	HOH407

---

site_id	AC3
Number of Residues	5
Details	binding site for residue PO4 A 203

Chain	Residue
A	LYS128
A	GNP201
A	HOH302
A	HOH360
A	HOH419

---

site_id	AC4
Number of Residues	25
Details	binding site for residue GNP B 201

Chain	Residue
B	GLY12
B	GLY13
B	VAL14
B	GLY15
B	LYS16
B	SER17
B	ALA18
B	PHE28
B	ARG34
B	GLY60
B	ASN116
B	LYS117
B	ASP119
B	LEU120
B	SER145
B	ALA146
B	LYS147
B	MG202
B	HOH303
B	HOH309
B	HOH317
B	HOH318
B	HOH331
B	HOH360
B	HOH369

---

site_id	AC5
Number of Residues	5
Details	binding site for residue MG B 202

Chain	Residue
B	SER17
B	GNP201
B	HOH309
B	HOH318
B	HOH331

---

site_id	AC6
Number of Residues	26
Details	binding site for residue GNP C 201

Chain	Residue
C	GLY12
C	GLY13
C	VAL14
C	GLY15
C	LYS16
C	SER17
C	ALA18
C	PHE28
C	GLU31
C	ARG34
C	GLY60
C	ASN116
C	LYS117
C	ASP119
C	LEU120
C	SER145
C	ALA146
C	LYS147
C	MG202
C	HOH303
C	HOH305
C	HOH307
C	HOH325
C	HOH327
C	HOH356
C	HOH358

---

site_id	AC7
Number of Residues	5
Details	binding site for residue MG C 202

Chain	Residue
C	HOH305
C	HOH325
C	HOH356
C	SER17
C	GNP201

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	Motif: {"description":"Effector region"}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	54
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	3
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	3
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	3
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	3
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

---