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Structure of PDB 7tcm Chain B

Receptor sequence
>7tcmB (length=372) Species: 470 (Acinetobacter baumannii) [Search protein sequence]
HHMKVGLVGWRGMVGSVLMQRMVEENDFAHIEPFYFSTSNAGGEAPSFGG
KTAPALMEATDITSLKQMDVIITCQGGDYTSEVFPKLKATGWDGYWIDAA
STLRMTDDAIIVLDPVNLNVIKDGLAKGTKTFVGGNCTVSLMLMGVGALF
QNNLVEWMTAMTYQAASGAGAQNMRELLTGMGYLYNNTKTLLDDPKSAIL
DIDRQVAELQRGEGFPSANFGVPLAGSLIPYIDKQLESGQSKEEWKGQVE
TNKILGNSQIVPIDGHCVRIGAMRCHSQALTIKLKKDVPLDEIEDMIRNS
NQWAKVVPNTREASMTDLTPVAVTGTLTVPVGRLRKLNMGKEYLGAFTVG
DQLLWGAAEPLRRMLRILVEYK
3D structure
PDB7tcm Crystal Structure of aspartate-semialdehyde dehydrogenase from Acinetobacter baumannii in complex with NADP
ChainB
Resolution1.95 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.2.1.11: aspartate-semialdehyde dehydrogenase.
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 NAP B G7 R9 G10 M11 V12 T36 S37 C72 Q73 G74 A98 S165 Q350 A355 G9 R11 G12 M13 V14 T38 S39 C74 Q75 G76 A100 S167 Q352 A357
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004073 aspartate-semialdehyde dehydrogenase activity
GO:0016491 oxidoreductase activity
GO:0016620 oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
GO:0046983 protein dimerization activity
GO:0050661 NADP binding
GO:0051287 NAD binding
Biological Process
GO:0006520 amino acid metabolic process
GO:0008652 amino acid biosynthetic process
GO:0009085 lysine biosynthetic process
GO:0009086 methionine biosynthetic process
GO:0009088 threonine biosynthetic process
GO:0009089 lysine biosynthetic process via diaminopimelate
GO:0009097 isoleucine biosynthetic process
GO:0019877 diaminopimelate biosynthetic process
GO:0071266 'de novo' L-methionine biosynthetic process

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External links

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