BioLiP

Structure of PDB 1dd7 Chain A

Receptor sequence

>1dd7A (length=295) Species: 10090 (Mus musculus) [Search protein sequence]

MNPKSLTRGPRDKPTPLEELLPHAIEFINQYYGSFKEAKIEEHLARLEAV
TKEIETTGTYQLTLDELIFATKMAWRNAPRCIGRIQWSNLQVFDARNCST
AQEMFQHICRHILYATNNGNIRSAITVFPQRSDGKHDFRLWNSQLIRYAG
YQTIRGDAATLEFTQLCIDLGWKPRYGRFDVLPLVLQADGQDPEVFEIPP
DLVLEVTMELGLKWYALPAVANMLLEVGGLEFPACPFNGWYMNVAVLHSF
QKQNVTIMDHHTASESFMKHMQNEYVLSPFYYYQIEPWKTHIWQN

3D structure

PDB

1dd7 Allosteric inhibitors of inducible nitric oxide synthase dimerization discovered via combinatorial chemistry.

Chain

Resolution

2.25 Å

3D
structure

Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]

Enzymatic activity

Catalytic site (original residue number in PDB)	C194 R197 W366
Catalytic site (residue number reindexed from 1)	C81 R84 W240
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	SO3	A	H440 N443 E444	H270 N273 E274
BS02	HEM	A	W188 A191 P192 R193 C194 G196 S236 F363 N364 G365 W366 M368 Y483 Y485	W75 A78 P79 R80 C81 G83 S123 F237 N238 G239 W240 M242 Y281 Y283
BS03	1PM	A	Q257 P344 V346 G365 W366 Y485	Q144 P218 V220 G239 W240 Y283	MOAD: ic50=28nM

Gene Ontology

	Molecular Function
GO:0004517	nitric-oxide synthase activity
GO:0020037	heme binding

	Biological Process
GO:0006809	nitric oxide biosynthetic process

View graph for
Molecular Function

View graph for
Biological Process

PDB	RCSB:1dd7, PDBe:1dd7, PDBj:1dd7
PDBsum	1dd7
PubMed	10677491
UniProt	P29477\|NOS2_MOUSE Nitric oxide synthase, inducible (Gene Name=Nos2)