9WR1

Ala/Ser-specific racemase in complex with PLP-L-Ala

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0008784	molecular_function	alanine racemase activity
A	0030170	molecular_function	pyridoxal phosphate binding
A	0030378	molecular_function	serine racemase activity
A	0042802	molecular_function	identical protein binding
B	0003824	molecular_function	catalytic activity
B	0008784	molecular_function	alanine racemase activity
B	0030170	molecular_function	pyridoxal phosphate binding
B	0030378	molecular_function	serine racemase activity
B	0042802	molecular_function	identical protein binding
C	0003824	molecular_function	catalytic activity
C	0008784	molecular_function	alanine racemase activity
C	0030170	molecular_function	pyridoxal phosphate binding
C	0030378	molecular_function	serine racemase activity
C	0042802	molecular_function	identical protein binding
D	0003824	molecular_function	catalytic activity
D	0008784	molecular_function	alanine racemase activity
D	0030170	molecular_function	pyridoxal phosphate binding
D	0030378	molecular_function	serine racemase activity
D	0042802	molecular_function	identical protein binding

Functional Information from PROSITE/UniProt

site_id	PS00600
Number of Residues	38
Details	AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LVmDEVqt.GIgRtGkwfasewfnvkp....DMIifGKgvaSG

Chain	Residue	Details
A	LEU259-GLY296

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P22256","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	4
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"UniProtKB","id":"P22256","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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