BioLiP

Structure of PDB 5g0p Chain A

Receptor sequence

>5g0pA (length=407) Species: 10116 (Rattus norvegicus) [Search protein sequence]

RFLKVKNWETDVVLTDTLHLKSTLETGCTEHICMGSIVLPTKDQLFPLAK
EFLDQYYSSIKRFGSKAHMDRLEEVNKEIESTSTYQLKDTELIYGAKHAW
RNASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLRSAI
TIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVQFTEICIQQG
WKAPRGRFDVLPLLLQANGNDPELFQIPPELVLEVPIRHPKFDWFKDLGL
KWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVRNYCDNSRYNILEE
VAKKMDLDMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATESFI
KHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEMLNYRLTPSFEYQPD
PWNTHVW

3D structure

PDB

5g0p Electrostatic Control of Isoform Selective Inhibitor Binding in Nitric Oxide Synthase.

Chain

Resolution

2.1 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	C415 R418 W587 E592
Catalytic site (residue number reindexed from 1)	C106 R109 W278 E283
Enzyme Commision number	1.14.13.39: nitric-oxide synthase (NADPH).

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	HEM	A	W409 C415 F584 W587 E592 F704 Y706	W100 C106 F275 W278 E283 F395 Y397
BS02	H4B	A	S334 R596 V677 W678	S36 R287 V368 W369
BS03	W67	A	Q478 P565 V567 F584 S585 W587 E592 Y706	Q169 P256 V258 F275 S276 W278 E283 Y397	MOAD: Ki=108nM BindingDB: Ki=25nM
BS04	ZN	A	C326 C331	C28 C33
BS05	H4B	A	F691 E694	F382 E385

Gene Ontology

	Molecular Function
GO:0004517	nitric-oxide synthase activity

	Biological Process
GO:0006809	nitric oxide biosynthetic process

View graph for
Molecular Function

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Biological Process

PDB	RCSB:5g0p, PDBe:5g0p, PDBj:5g0p
PDBsum	5g0p
PubMed	27250740
UniProt	P29476\|NOS1_RAT Nitric oxide synthase 1 (Gene Name=Nos1)