Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6P8X

Crystal structure of human KRAS G12C covalently bound to an acryloylazetidine acetamide inhibitor.

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue CA A 301

Chain	Residue
A	SER17
A	GDP304
A	HOH413
A	HOH421
A	HOH425
A	HOH442

site_id	AC2
Number of Residues	5
Details	binding site for residue CA A 302

Chain	Residue
A	HOH423
A	HOH452
A	GLU63
A	GLY138
A	HOH422

site_id	AC3
Number of Residues	5
Details	binding site for residue CA A 303

Chain	Residue
A	ASP105
A	HOH428
A	HOH445
C	HOH402
C	HOH421

site_id	AC4
Number of Residues	22
Details	binding site for residue GDP A 304

Chain	Residue
A	GLY13
A	VAL14
A	GLY15
A	LYS16
A	SER17
A	ALA18
A	PHE28
A	VAL29
A	ASP30
A	ASN116
A	LYS117
A	ASP119
A	SER145
A	ALA146
A	LYS147
A	CA301
A	O5V305
A	HOH404
A	HOH413
A	HOH440
A	HOH442
C	MET1

site_id	AC5
Number of Residues	18
Details	binding site for residue O5V A 305

Chain	Residue
A	GLY10
A	CYS12
A	LYS16
A	PRO34
A	ALA59
A	GLY60
A	GLN61
A	MET72
A	ASP92
A	HIS95
A	TYR96
A	GLN99
A	ILE100
A	GDP304
A	HOH414
A	HOH442
D	HIS95
D	O5V304

site_id	AC6
Number of Residues	6
Details	binding site for residue CA B 301

Chain	Residue
B	SER17
B	GDP304
B	HOH410
B	HOH412
B	HOH413
B	HOH429

site_id	AC7
Number of Residues	5
Details	binding site for residue CA B 302

Chain	Residue
B	GLU63
B	GLY138
B	HOH417
B	HOH421
B	HOH440

site_id	AC8
Number of Residues	5
Details	binding site for residue CA B 303

Chain	Residue
B	ASP105
B	HOH411
D	HOH401
D	HOH406
D	HOH445

site_id	AC9
Number of Residues	22
Details	binding site for residue GDP B 304

Chain	Residue
B	GLY13
B	VAL14
B	GLY15
B	LYS16
B	SER17
B	ALA18
B	PHE28
B	VAL29
B	ASP30
B	ASN116
B	LYS117
B	ASP119
B	LEU120
B	SER145
B	ALA146
B	LYS147
B	CA301
B	O5V305
B	HOH412
B	HOH429
B	HOH433
D	MET1

site_id	AD1
Number of Residues	6
Details	binding site for residue CA C 301

Chain	Residue
C	HOH437
C	SER17
C	GDP303
C	HOH408
C	HOH413
C	HOH417

site_id	AD2
Number of Residues	6
Details	binding site for residue CA C 302

Chain	Residue
C	GLU63
C	GLY138
C	HOH404
C	HOH407
C	HOH427
C	HOH432

site_id	AD3
Number of Residues	20
Details	binding site for residue GDP C 303

Chain	Residue
C	GLY13
C	VAL14
C	GLY15
C	LYS16
C	SER17
C	ALA18
C	PHE28
C	VAL29
C	ASP30
C	ASN116
C	LYS117
C	ASP119
C	LEU120
C	SER145
C	ALA146
C	LYS147
C	CA301
C	HOH413
C	HOH420
C	HOH437

site_id	AD4
Number of Residues	6
Details	binding site for residue CA D 301

Chain	Residue
D	SER17
D	GDP303
D	HOH407
D	HOH423
D	HOH429
D	HOH439

site_id	AD5
Number of Residues	6
Details	binding site for residue CA D 302

Chain	Residue
D	GLU63
D	GLY138
D	HOH403
D	HOH421
D	HOH447
D	HOH456

site_id	AD6
Number of Residues	21
Details	binding site for residue GDP D 303

Chain	Residue
D	GLY13
D	VAL14
D	GLY15
D	LYS16
D	SER17
D	ALA18
D	PHE28
D	VAL29
D	ASP30
D	ASN116
D	LYS117
D	ASP119
D	LEU120
D	SER145
D	ALA146
D	LYS147
D	CA301
D	O5V304
D	HOH429
D	HOH439
D	HOH440

site_id	AD7
Number of Residues	22
Details	binding site for Di-peptide O5V B 305 and CYS B 12

Chain	Residue
B	GLY10
B	ALA11
B	GLY13
B	VAL14
B	LYS16
B	PRO34
B	ALA59
B	GLY60
B	GLN61
B	GLU63
B	MET72
B	ASP92
B	HIS95
B	TYR96
B	GLN99
B	ILE100
B	GDP304
B	HOH415
B	HOH425
B	HOH429
C	HIS95
C	O5V304

site_id	AD8
Number of Residues	17
Details	binding site for Di-peptide O5V C 304 and CYS C 12

Chain	Residue
B	HIS95
B	O5V305
C	GLY10
C	ALA11
C	GLY13
C	VAL14
C	LYS16
C	ALA59
C	GLY60
C	ARG68
C	MET72
C	ASP92
C	HIS95
C	TYR96
C	GLN99
C	ILE100
C	HOH428

site_id	AD9
Number of Residues	19
Details	binding site for Di-peptide O5V D 304 and CYS D 12

Chain	Residue
A	HIS95
A	O5V305
D	GLY10
D	ALA11
D	GLY13
D	VAL14
D	LYS16
D	ALA59
D	GLY60
D	GLN61
D	ARG68
D	MET72
D	ASP92
D	TYR96
D	ILE100
D	GDP303
D	HOH430
D	HOH439
D	HOH446

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	16
Details	BINDING: BINDING => ECO:0000269\|PubMed:22431598, ECO:0000269\|PubMed:22566140

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

site_id	SWS_FT_FI2
Number of Residues	4
Details	MOD_RES: N-acetylmethionine; in GTPase KRas; alternate => ECO:0000269\|Ref.17

Chain	Residue	Details
A	MET1
B	MET1
C	MET1
D	MET1

site_id	SWS_FT_FI3
Number of Residues	4
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

site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: N6-acetyllysine => ECO:0000269\|PubMed:22711838

Chain	Residue	Details
A	LYS104
B	LYS104
C	LYS104
D	LYS104

site_id	SWS_FT_FI5
Number of Residues	4
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

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