Structure of PDB 1upb Chain D

Receptor sequence
>1upbD (length=558) Species: 1901 (Streptomyces clavuligerus) [Search protein sequence]
PTAAHALLSRLRDHGVGKVFGVVGREAASILFDEVEGIDFVLTRHEFTAG
VAADVLARITGRPQACWATLGPGMTNLSTGIATSVLDRSPVIALAAQSES
HDIFPNDTHQCLDSVAIVAPMSKYAVELQRPHEITDLVDSAVNAAMTEPV
GPSFISLPVDLLGSSEGIDTNPPANTPAKPVGVVADGWQKAADQAAALLA
EAKHPVLVVGAAAIRSGAVPAIRALAERLNIPVITTYIAKGVLPVGHELN
YGAVTGYMDGILNFPALQTMFAPVDLVLTVGYDYAEDLRPSMWQKGIEKK
TVRISPTVNPIPRVYRPDVDVVTDVLAFVEHFETATASFGAKQRHDIEPL
RARIAEFLADPETYEDGMRVHQVIDSMNTVMEEAAEPGEGTIVSDIGFFR
HYGVLFARADQPFGFLTSAGCSSFGYGIPAAIGAQMARPDQPTFLIAGDG
GFHSNSSDLETIARLNLPIVTVVVNNDTNGLIELYQNIGHHRSHDPAVKF
GGVDFVALAEANGVDATRATNREELLAALRKGAELGRPFLIEVPVNYDFQ
PGGFGALS
3D structure
PDB1upb Crystal Structure and Mechanistic Implications of N2-(2-Carboxyethyl)Arginine Synthase, the First Enzyme in the Clavulanic Acid Biosynthesis Pathway
ChainD
Resolution2.35 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) V22 G24 R25 E26 A27 E46 T69 H109 Q110 C111 V159 I261 L288 I396 S422 F424 D449 N476 T478 N479 L481 I482 Y485 Y547
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 TPP D I410 G411 F412 F413 F438 G462 D463 G464 G465 T492 N493 G494 L495 Y561 I396 G397 F398 F399 F424 G448 D449 G450 G451 T478 N479 G480 L481 Y547
BS02 MG D D463 N490 T492 D449 N476 T478
BS03 SO4 D Y271 R414 H415 Y257 R400 H401
BS04 SO4 D N490 N560 Y561 N476 N546 Y547
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:1upb, PDBe:1upb, PDBj:1upb
PDBsum1upb
PubMed14623876
UniProtQ9LCV9|CEAS_STRCL N(2)-(2-carboxyethyl)arginine synthase (Gene Name=ceaS)

[Back to BioLiP]