Structure of PDB 3a8u Chain X

Receptor sequence
>3a8uX (length=441) Species: 303 (Pseudomonas putida) [Search protein sequence]
ASLASQLKLDAHWMPYTANRNFLRDPRLIVAAEGSWLVDDKGRKVYDSLS
GLWTCGAGHTRKEIQEAVAKQLSTLDYSPGFQYGHPLSFQLAEKITDLTP
GNLNHVFFTDSGSECALTAVKMVRAYWRLKGQATKTKMIGRARGYHGVNI
AGTSLGGVNGNRKLFGQPMQDVDHLPHTLLASNAYSRGMPKEGGIALADE
LLKLIELHDASNIAAVFVEPLAGSAGVLVPPEGYLKRNREICNQHNILLV
FDEVITGFGRTGSMFGADSFGVTPDLMCIAKQVTNGAIPMGAVIASTEIY
QTFMNQPTPEYAVEFPHGYTYSAHPVACAAGLAALCLLQKENLVQSVAEV
APHFEKALHGIKGAKNVIDIRNFGLAGAIQIAPRDGDAIVRPFEAGMALW
KAGFYVRFGGDTLQFGPTFNSKPQDLDRLFDAVGEVLNKLL
3D structure
PDB3a8u Crystal structure analysis of omega-amino acid:pyruvate aminotransferase with a newly developed Weissenberg camera and an imaging plate using synchrotron radiation
ChainX
Resolution1.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y152 D259 K288 Q421
Catalytic site (residue number reindexed from 1) Y145 D252 K281 Q414
Enzyme Commision number 2.6.1.18: beta-alanine--pyruvate transaminase.
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 PLP X S118 G119 S120 Y152 H153 G154 E226 D259 V261 I262 K288 S111 G112 S113 Y145 H146 G147 E219 D252 V254 I255 K281
Gene Ontology
Molecular Function
GO:0004015 adenosylmethionine-8-amino-7-oxononanoate transaminase activity
GO:0008483 transaminase activity
GO:0016223 beta-alanine:pyruvate transaminase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0009102 biotin biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3a8u, PDBe:3a8u, PDBj:3a8u
PDBsum3a8u
PubMed
UniProtP28269|OAPT_PSEPU Omega-amino acid--pyruvate aminotransferase

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