Structure of PDB 2ihu Chain D

Receptor sequence
>2ihuD (length=551) Species: 1901 (Streptomyces clavuligerus) [Search protein sequence]
KPTAAHALLSRLRDHGVGKVFGVVGREAASILFDEVEGIDFVLTRHEFTA
GVAADVLARITGRPQACWATLGPGMTNLSTGIATSVLDRSPVIALAAQSE
SHDIFPNDTHQCLDSVAIVAPMSKYAVELQRPHEITDLVDSAVNAAMTEP
VGPSFISLPVDLLGSSEGIDTTVPNPPANTPAKPVGVVADGWQKAADQAA
ALLAEAKHPVLVVGAAAIRSGAVPAIRALAERLNIPVITTYIAKGVLPVG
HELNYGAVTGYMDGILNFPALQTMFAPVDLVLTVGYDYAEDLRPSMWQKG
IEKKTVRISPTVNPIPRVYRPDVDVVTDVLAFVEHFETATASFGAKQRHD
IEPLRARIAEFLADPETYEDGMRVHQVIDSMNTVMEEAAEPGEGTIVSDI
GFFRHYGVLFARADQPFGFLTSAGCSSFGYGIPAAIGAQMARPDQPTFLI
AGDGGFHSNSSDLETIARLNLPIVTVVVNNDTNGLIELYQNIGHHRSHDP
AVKFGGVDFVALAEANGVDATRATNREELLAALRKGAELGRPFLIEVPVN
Y
3D structure
PDB2ihu Structural and mechanistic studies on N(2)-(2-carboxyethyl)arginine synthase.
ChainD
Resolution2.05 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) V33 G35 R36 E37 A38 E57 T80 H120 Q121 C122 V170 I275 L302 I410 S436 F438 D463 N490 T492 N493 L495 I496 Y499 Y561
Catalytic site (residue number reindexed from 1) V23 G25 R26 E27 A28 E47 T70 H110 Q111 C112 V160 I265 L292 I400 S426 F428 D453 N480 T482 N483 L485 I486 Y489 Y551
Enzyme Commision number 2.5.1.66: N(2)-(2-carboxyethyl)arginine synthase.
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 TP8 D E57 T80 H120 E47 T70 H110
BS02 MG D D463 N490 T492 D453 N480 T482
BS03 TP9 D I410 G411 F412 F413 S437 F438 G462 D463 G464 G465 T492 N493 G494 L495 I496 Y561 I400 G401 F402 F403 S427 F428 G452 D453 G454 G455 T482 N483 G484 L485 I486 Y551
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003824 catalytic activity
GO:0003984 acetolactate synthase activity
GO:0016740 transferase activity
GO:0030976 thiamine pyrophosphate binding
GO:0033848 N2-(2-carboxyethyl)arginine synthase activity
GO:0046872 metal ion binding
GO:0050660 flavin adenine dinucleotide binding
Biological Process
GO:0009097 isoleucine biosynthetic process
GO:0009099 L-valine biosynthetic process
Cellular Component
GO:0005948 acetolactate synthase complex

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2ihu, PDBe:2ihu, PDBj:2ihu
PDBsum2ihu
PubMed19477162
UniProtQ9LCV9|CEAS_STRCL N(2)-(2-carboxyethyl)arginine synthase (Gene Name=ceaS)

[Back to BioLiP]