Structure of PDB 3r6q Chain H

Receptor sequence
>3r6qH (length=462) Species: 96471 (Bacillus sp. YM55-1) [Search protein sequence]
VRIEKDFLGEKEIPKDAYYGVQTIRATENFPITGYRIHPELIKSLGIVKK
SAALANMEVGLLDKEVGQYIVKAADEVIEGKWNDQFIVDPIQGGAGTSIN
MNANEVIANRALELMGEEKGNYSKISPNSHVNMSQSTNDAFPTATHIAVL
SLLNQLIETTKYMQQEFMKKADEFAGVIKMGRTHLQDAVPILLGQEFEAY
ARVIARDIERIANTRNNLYDINMGATAVGTGLNADPEYISIVTEHLAKFS
GHPLRSAQHLVDATQNTDCYTEVSSALKVCMINMSKIANDLRLMASGPRA
GLSEIVLPARQPGSSIMPGKVNPVMPEVMNQVAFQVFGNDLTITSASEAG
QFELNVMEPVLFFNLIQSISIMTNVFKSFTENCLKGIKANEERMKEYVEK
SIGIITAINPHVGYETAAKLAREAYLTGESIRELCIKYGVLTEEQLNEIL
NPYEMIHPGIAG
3D structure
PDB3r6q Structural basis for the catalytic mechanism of aspartate ammonia lyase.
ChainH
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H188 S318 K324 E331
Catalytic site (residue number reindexed from 1) H184 S314 K320 E327
Enzyme Commision number 4.3.1.1: aspartate ammonia-lyase.
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 CA H A393 E395 A389 E391
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0008797 aspartate ammonia-lyase activity
GO:0016829 lyase activity
Biological Process
GO:0006099 tricarboxylic acid cycle
GO:0006531 aspartate metabolic process
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3r6q, PDBe:3r6q, PDBj:3r6q
PDBsum3r6q
PubMed21661762
UniProtQ9LCC6|ASPA_BACSP Aspartate ammonia-lyase (Gene Name=aspB)

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