Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3EJ8

Structure of double mutant of human iNOS oxygenase domain with bound immidazole

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004517	molecular_function	nitric-oxide synthase activity
A	0006809	biological_process	nitric oxide biosynthetic process
B	0004517	molecular_function	nitric-oxide synthase activity
B	0006809	biological_process	nitric oxide biosynthetic process
C	0004517	molecular_function	nitric-oxide synthase activity
C	0006809	biological_process	nitric oxide biosynthetic process
D	0004517	molecular_function	nitric-oxide synthase activity
D	0006809	biological_process	nitric oxide biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE HEC A1901

Chain	Residue
A	TRP194
A	GLU377
A	TRP463
A	TYR489
A	TYR491
A	H4B1902
A	IMD1904
A	ARG199
A	CYS200
A	GLN205
A	SER242
A	PHE369
A	ASN370
A	GLY371
A	TRP372

site_id	AC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE H4B A1902

Chain	Residue
A	SER118
A	MET120
A	ARG381
A	ILE462
A	TRP463
A	HEC1901
A	HOH5031
B	TRP461
B	PHE476
B	HIS477
B	GLN478

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A1903

Chain	Residue
A	CYS110
A	CYS115
B	CYS110
B	CYS115

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE IMD A1904

Chain	Residue
A	TRP372
A	GLU377
A	HEC1901

site_id	AC5
Number of Residues	13
Details	BINDING SITE FOR RESIDUE HEC B2901

Chain	Residue
B	TRP194
B	CYS200
B	GLN205
B	PHE369
B	GLY371
B	TRP372
B	GLU377
B	MET434
B	TRP463
B	TYR489
B	TYR491
B	H4B2902
B	IMD2904

site_id	AC6
Number of Residues	10
Details	BINDING SITE FOR RESIDUE H4B B2902

Chain	Residue
A	TRP461
A	PHE476
A	HIS477
A	GLN478
B	SER118
B	MET120
B	ARG381
B	ILE462
B	TRP463
B	HEC2901

site_id	AC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE IMD B2904

Chain	Residue
B	GLU377
B	HEC2901

site_id	AC8
Number of Residues	16
Details	BINDING SITE FOR RESIDUE HEC C3901

Chain	Residue
C	TRP194
C	ARG199
C	CYS200
C	GLY202
C	GLN205
C	MET355
C	PHE369
C	ASN370
C	GLY371
C	TRP372
C	GLU377
C	TRP463
C	TYR489
C	TYR491
C	H4B3902
C	IMD3904

site_id	AC9
Number of Residues	8
Details	BINDING SITE FOR RESIDUE H4B C3902

Chain	Residue
C	SER118
C	MET120
C	ARG381
C	ILE462
C	TRP463
C	HEC3901
D	TRP461
D	PHE476

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C3903

Chain	Residue
C	CYS110
C	CYS115
D	CYS110
D	CYS115

site_id	BC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE IMD C3904

Chain	Residue
C	GLU377
C	HEC3901

site_id	BC3
Number of Residues	12
Details	BINDING SITE FOR RESIDUE HEC D4901

Chain	Residue
D	IMD4904
D	TRP194
D	CYS200
D	GLN205
D	PHE369
D	GLY371
D	TRP372
D	GLU377
D	TRP463
D	TYR489
D	TYR491
D	H4B4902

site_id	BC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE H4B D4902

Chain	Residue
C	TRP90
C	TRP461
C	PHE476
C	HIS477
C	GLN478
D	SER118
D	MET120
D	ARG381
D	ILE462
D	TRP463
D	HEC4901
D	HOH5166

site_id	BC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE IMD D4904

Chain	Residue
D	GLU377
D	HEC4901
D	HOH5071

Functional Information from PROSITE/UniProt

site_id	PS60001
Number of Residues	8
Details	NOS Nitric oxide synthase (NOS) signature. RCIGRIqW

Chain	Residue	Details
A	ARG199-TRP206

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269\|PubMed:10074942, ECO:0000269\|PubMed:10409685, ECO:0007744\|PDB:1NSI, ECO:0007744\|PDB:4NOS

Chain	Residue	Details
A	CYS110
A	CYS115
B	CYS110
B	CYS115
C	CYS110
C	CYS115
D	CYS110
D	CYS115

site_id	SWS_FT_FI2
Number of Residues	24
Details	BINDING: BINDING => ECO:0000269\|PubMed:10074942, ECO:0000269\|PubMed:10409685, ECO:0007744\|PDB:1NSI, ECO:0007744\|PDB:2NSI, ECO:0007744\|PDB:4NOS

Chain	Residue	Details
A	SER118
B	TRP463
B	PHE476
B	TYR491
C	SER118
C	ARG381
C	ILE462
C	TRP463
C	PHE476
C	TYR491
D	SER118
A	ARG381
D	ARG381
D	ILE462
D	TRP463
D	PHE476
D	TYR491
A	ILE462
A	TRP463
A	PHE476
A	TYR491
B	SER118
B	ARG381
B	ILE462

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: axial binding residue => ECO:0000269\|PubMed:10074942, ECO:0000269\|PubMed:10409685, ECO:0007744\|PDB:1NSI, ECO:0007744\|PDB:2NSI, ECO:0007744\|PDB:4NOS

Chain	Residue	Details
A	CYS200
B	CYS200
C	CYS200
D	CYS200

site_id	SWS_FT_FI4
Number of Residues	16
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:P29474

Chain	Residue	Details
A	GLN263
C	TRP372
C	TYR373
C	GLU377
D	GLN263
D	TRP372
D	TYR373
D	GLU377
A	TRP372
A	TYR373
A	GLU377
B	GLN263
B	TRP372
B	TYR373
B	GLU377
C	GLN263

site_id	SWS_FT_FI5
Number of Residues	4
Details	MOD_RES: Phosphoserine; by PKA => ECO:0000255

Chain	Residue	Details
A	SER234
B	SER234
C	SER234
D	SER234

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 3nos

Chain	Residue	Details
A	TRP372
A	CYS200
A	GLU377
A	ARG203

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 3nos

Chain	Residue	Details
B	TRP372
B	CYS200
B	GLU377
B	ARG203

site_id	CSA3
Number of Residues	4
Details	Annotated By Reference To The Literature 3nos

Chain	Residue	Details
C	TRP372
C	CYS200
C	GLU377
C	ARG203

site_id	CSA4
Number of Residues	4
Details	Annotated By Reference To The Literature 3nos

Chain	Residue	Details
D	TRP372
D	CYS200
D	GLU377
D	ARG203

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