Structure of PDB 1mmw Chain A

Receptor sequence
>1mmwA (length=407) Species: 10116 (Rattus norvegicus) [Search protein sequence]
RFLKVKNWETDVVLTDTLHLKSTLETGCTEHICMGSIMLPTKDQLFPLAK
EFLDQYYSSIKRFGSKAHMDRLEEVNKEIESTSTYQLKDTELIYGAKHAW
RNASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLRSAI
TIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVQFTEICIQQG
WKAPRGRFDVLPLLLQANGNDPELFQIPPELVLEVPIRHPKFDWFKDLGL
KWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVRDYCDNSRYNILEE
VAKKMDLDMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATESFI
KHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEMLNYRLTPSFEYQPD
PWNTHVW
3D structure
PDB1mmw Structural characterization and kinetics of nitric-oxide synthase inhibition by novel N5-(iminoalkyl)- and N5-(iminoalkenyl)-ornithines
ChainA
Resolution2.0 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 ZN A C326 C331 C28 C33
BS02 HEM A W409 C415 V416 F584 S585 W587 E592 W678 F704 Y706 W100 C106 V107 F275 S276 W278 E283 W369 F395 Y397
BS03 H4B A S334 R596 V677 W678 S36 R287 V368 W369
BS04 VIO A Q478 P565 V567 F584 Y588 E592 D597 Q169 P256 V258 F275 Y279 E283 D288
BS05 H4B A F691 H692 E694 F382 H383 E385
Gene Ontology
Molecular Function
GO:0004517 nitric-oxide synthase activity
GO:0020037 heme binding
Biological Process
GO:0006809 nitric oxide biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1mmw, PDBe:1mmw, PDBj:1mmw
PDBsum1mmw
PubMed12960153
UniProtP29476|NOS1_RAT Nitric oxide synthase 1 (Gene Name=Nos1)

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