Structure of PDB 1j32 Chain B

Receptor sequence
>1j32B (length=388) Species: 32060 (Phormidium lapideum) [Search protein sequence]
MKLAARVESVSPSMTLIIDAKAKAMKAEGIDVCSFSAGEPDFNTPKHIVE
AAKAALEQGKTRYGPAAGEPRLREAIAQKLQRDNGLCYGADNILVTNGGK
QSIFNLMLAMIEPGDEVIIPAPFWVSYPEMVKLAEGTPVILPTTVETQFK
VSPEQIRQAITPKTKLLVFNTPSNPTGMVYTPDEVRAIAQVAVEAGLWVL
SDEIYEKILYDDAQHLSIGAASPEAYERSVVCSGFAKTYAMTGWRVGFLA
GPVPLVKAATKIQGHSTSNVCTFAQYGAIAAYENSQDCVQEMLAAFAERR
RYMLDALNAMPGLECPKPDGAFYMFPSIAKTGRSSLDFCSELLDQHQVAT
VPGAAFGADDCIRLSYATDLDTIKRGMERLEKFLHGIL
3D structure
PDB1j32 Structural studies of aspartate aminotransferase from Phormidium lapideum
ChainB
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) W124 D202 I204 K237
Catalytic site (residue number reindexed from 1) W124 D202 I204 K237
Enzyme Commision number 2.6.1.-
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 B G98 G99 K100 W124 N170 N174 D202 I204 Y205 A236 K237 R245 G98 G99 K100 W124 N170 N174 D202 I204 Y205 A236 K237 R245
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0008483 transaminase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0006520 amino acid metabolic process
GO:0009058 biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1j32, PDBe:1j32, PDBj:1j32
PDBsum1j32
PubMed
UniProtQ8RR70

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