Structure of PDB 4cul Chain A

Receptor sequence
>4culA (length=386) Species: 9913 (Bos taurus) [Search protein sequence]
GPKFPRVKNWELGSITYDTLCAQSPAEQLLSQARDFINQYYSSIKRSGSQ
AHEERLQEVEAEVASTGTYHLRESELVFGAKQAWRNAPRCVGRIQWGKLQ
VFDARDCSSAQEMFTYICNHIKYATNRGNLRSAITVFPQRAPGRGDFRIW
NSQLVRYAGYRQQDGSVRGDPANVEITELCIQHGWTPGNGRFDVLPLLLQ
APDEAPELFVLPPELVLEVPLEHPTLEWFAALGLRWYALPAVSNMLLEIG
GLEFSAAPFSGWYMSTEIGTRNLCDPHRYNILEDVAVCMDLDTRTTSSLW
KDKAAVEINLAVLHSFQLAKVTIVDHHAATVSFMKHLDNEQKARGGCPAD
WAWIVPPISGSLTPVFHQEMVNYILSPAFRYQPDPW
3D structure
PDB4cul Communication between the Zinc and Tetrahydrobiopterin Binding Sites in Nitric Oxide Synthase.
ChainA
Resolution2.23 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C186 R189 W358 E363
Catalytic site (residue number reindexed from 1) C90 R93 W262 E267
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 ARG A Q249 P336 Y359 E363 N368 Q153 P240 Y263 E267 N272
BS02 HEM A W180 C186 V187 F355 G357 W358 E363 W449 F475 Y477 W84 C90 V91 F259 G261 W262 E267 W353 F379 Y381
BS03 WSD A R367 A448 W449 R271 A352 W353
BS04 WSD A W447 F462 W351 F366
Gene Ontology
Molecular Function
GO:0004517 nitric-oxide synthase activity
Biological Process
GO:0006809 nitric oxide biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4cul, PDBe:4cul, PDBj:4cul
PDBsum4cul
PubMed24819538
UniProtP29473|NOS3_BOVIN Nitric oxide synthase 3 (Gene Name=NOS3)

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