Structure of PDB 3inn Chain D

Receptor sequence
>3innD (length=277) Species: 29459 (Brucella melitensis) [Search protein sequence]
SMQIIHTIEELRQALAPARQQGKKIGFVPTMGYLHKGHLELVRRARVEND
VTLVSIFVNPLQFGANDLERDAGLLHDAQVDYLFAPTVSDMYPRPMQTVV
DVPPLGNQIEGEPGHFAGVATVVSKLFNIVGPDAAYFGEKDFQQLVIIRR
MVDDMAIPVRIVGVETVREDDGLACSSRNVYLTPEQRRAAIIVPQALDEA
DRLYRSGMDDPDALEAAIRTFIGRQPLAVPEVIAIRDPETLERLPALQGR
PILVALFVRVGATRLLDNRVIGHAAPQ
3D structure
PDB3inn Crystal structure of pantoate-beta-alanine-ligase in complex with ATP at low occupancy at 2.1 A resolution
ChainD
Resolution2.1 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) M30 H34 H37 R77 D78 L81 K149 S185 S186 R187
Catalytic site (residue number reindexed from 1) M31 H35 H38 R70 D71 L74 K140 S176 S177 R178
Enzyme Commision number 6.3.2.1: pantoate--beta-alanine ligase (AMP-forming).
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 ATP D T29 M30 H34 H37 L40 F146 G147 D150 T175 V176 C184 T30 M31 H35 H38 L41 F137 G138 D141 T166 V167 C175
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004592 pantoate-beta-alanine ligase activity
GO:0005524 ATP binding
GO:0016874 ligase activity
Biological Process
GO:0009058 biosynthetic process
GO:0015940 pantothenate biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:3inn, PDBe:3inn, PDBj:3inn
PDBsum3inn
PubMed
UniProtQ8YFC9|PANC_BRUME Pantothenate synthetase (Gene Name=panC)

[Back to BioLiP]