Structure of PDB 1df1 Chain A

Receptor sequence
>1df1A (length=420) Species: 10090 (Mus musculus) [Search protein sequence]
QYVRIKNWGSGEILHDTLHHKATSDFTCKSKSCLGSIMNPKSLTRGPRDK
PTPLEELLPHAIEFINQYYGSFKEAKIEEHLARLEAVTKEIETTGTYQLT
LDELIFATKMAWRNAPRCIGRIQWSNLQVFDARNCSTAQEMFQHICRHIL
YATNNGNIRSAITVFPQRSDGKHDFRLWNSQLIRYAGYQMPDGTIRGDAA
TLEFTQLCIDLGWKPRYGRFDVLPLVLQADGQDPEVFEIPPDLVLEVTME
HPKYEWFQELGLKWYALPAVANMLLEVGGLEFPACPFNGWYMGTEIGVRD
FCDTQRYNILEEVGRRMGLETHTLASLWKDRAVTEINVAVLHSFQKQNVT
IMDHHTASESFMKHMQNEYRARGGCPADWIWLVPPVSGSITPVFHQEMLN
YVLSPFYYYQIEPWKTHIWQ
3D structure
PDB1df1 N-terminal domain swapping and metal ion binding in nitric oxide synthase dimerization.
ChainA
Resolution2.35 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C194 R197 W366 E371
Catalytic site (residue number reindexed from 1) C118 R121 W290 E295
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 ZN A C104 C109 C28 C33
BS02 HEM A W188 C194 G196 S236 F363 N364 G365 W366 E371 W457 Y485 W112 C118 G120 S160 F287 N288 G289 W290 E295 W381 Y409
BS03 H4B A S112 R375 I456 W457 S36 R299 I380 W381
BS04 ITU A P344 V346 F363 W366 E371 P268 V270 F287 W290 E295 BindingDB: Ki=5.2nM
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:1df1, PDBe:1df1, PDBj:1df1
PDBsum1df1
PubMed10562539
UniProtP29477|NOS2_MOUSE Nitric oxide synthase, inducible (Gene Name=Nos2)

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