Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4NOS

HUMAN INDUCIBLE NITRIC OXIDE SYNTHASE WITH INHIBITOR

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	4
Details	BINDING SITE FOR RESIDUE ZN A 3000

Chain	Residue
A	CYS110
A	CYS115
B	CYS110
B	CYS115

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 2000

Chain	Residue
C	CYS110
C	CYS115
D	CYS110
D	CYS115

site_id	AC3
Number of Residues	20
Details	BINDING SITE FOR RESIDUE HEM A 510

Chain	Residue
A	TRP194
A	ARG199
A	CYS200
A	GLN205
A	SER242
A	PHE369
A	ASN370
A	TRP372
A	GLU377
A	TRP463
A	TYR489
A	TYR491
A	H2B511
A	ITU512
A	HOH3007
A	HOH3103
A	HOH3131
A	HOH3133
A	HOH3203
A	HOH3219

site_id	AC4
Number of Residues	15
Details	BINDING SITE FOR RESIDUE H2B A 511

Chain	Residue
A	SER118
A	ARG381
A	ILE462
A	TRP463
A	HEM510
A	HOH3001
A	HOH3013
A	HOH3017
A	HOH3131
A	HOH3221
B	TRP461
B	PHE476
B	HIS477
B	GLN478
B	GLU479

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ITU A 512

Chain	Residue
A	PHE369
A	TRP372
A	GLU377
A	HEM510

site_id	AC6
Number of Residues	20
Details	BINDING SITE FOR RESIDUE HEM B 1010

Chain	Residue
B	TRP194
B	ARG199
B	CYS200
B	GLN205
B	LEU209
B	SER242
B	PHE369
B	ASN370
B	TRP372
B	MET374
B	GLU377
B	TRP463
B	TYR489
B	TYR491
B	H4B1011
B	ITU1012
B	HOH1059
B	HOH1074
B	HOH1143
B	HOH1144

site_id	AC7
Number of Residues	16
Details	BINDING SITE FOR RESIDUE H4B B 1011

Chain	Residue
A	TRP461
A	PHE476
A	HIS477
A	GLN478
A	GLU479
B	SER118
B	MET120
B	ARG381
B	ILE462
B	TRP463
B	HEM1010
B	HOH1018
B	HOH1021
B	HOH1056
B	HOH1113
B	HOH1144

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ITU B 1012

Chain	Residue
B	VAL352
B	PHE369
B	TRP372
B	GLU377
B	HEM1010

site_id	AC9
Number of Residues	19
Details	BINDING SITE FOR RESIDUE HEM C 2010

Chain	Residue
C	ASN370
C	TRP372
C	GLU377
C	TRP463
C	TYR491
C	H4B2011
C	ITU2012
C	HOH2041
C	HOH2075
C	HOH2142
C	HOH2161
C	HOH2164
C	HOH2173
C	TRP194
C	ARG199
C	CYS200
C	GLN205
C	SER242
C	PHE369

site_id	BC1
Number of Residues	16
Details	BINDING SITE FOR RESIDUE H4B C 2011

Chain	Residue
C	SER118
C	ARG381
C	ILE462
C	TRP463
C	HEM2010
C	HOH2015
C	HOH2016
C	HOH2044
C	HOH2056
C	HOH2115
C	HOH2142
D	TRP461
D	PHE476
D	HIS477
D	GLN478
D	GLU479

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ITU C 2012

Chain	Residue
C	PRO350
C	PHE369
C	TRP372
C	GLU377
C	HEM2010
C	HOH2214

site_id	BC3
Number of Residues	20
Details	BINDING SITE FOR RESIDUE HEM D 3010

Chain	Residue
D	TRP194
D	ARG199
D	CYS200
D	GLN205
D	SER242
D	PHE369
D	ASN370
D	GLY371
D	TRP372
D	MET374
D	GLU377
D	TRP463
D	TYR489
D	TYR491
D	H4B3011
D	ITU3012
D	HOH3056
D	HOH3060
D	HOH3137
D	HOH3153

site_id	BC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE H4B D 3011

Chain	Residue
C	TRP461
C	PHE476
C	HIS477
C	GLN478
D	SER118
D	ARG381
D	ILE462
D	TRP463
D	HEM3010
D	HOH3014
D	HOH3021
D	HOH3052

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ITU D 3012

Chain	Residue
D	VAL352
D	PHE369
D	TRP372
D	GLU377
D	HEM3010

site_id	COF
Number of Residues	2
Details	COFACTORS

Chain	Residue
A	HEM510
A	H2B511

site_id	SUB
Number of Residues	1
Details	INHIBITOR

Chain	Residue
A	ITU512

site_id	ZNB
Number of Residues	2
Details	ZN BINDING SITE AT THE DIMERIZATION INTERFACE 2 MOTIFS CX4C

Chain	Residue
A	CYS110
A	CYS115

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)