9J50

Crystal structure of the closed state of the omega transaminase TA_5182 from Pseudomonas putida KT2440

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008483	molecular_function	transaminase activity
A	0009447	biological_process	putrescine catabolic process
A	0030170	molecular_function	pyridoxal phosphate binding
B	0008483	molecular_function	transaminase activity
B	0009447	biological_process	putrescine catabolic process
B	0030170	molecular_function	pyridoxal phosphate binding
C	0008483	molecular_function	transaminase activity
C	0009447	biological_process	putrescine catabolic process
C	0030170	molecular_function	pyridoxal phosphate binding
D	0008483	molecular_function	transaminase activity
D	0009447	biological_process	putrescine catabolic process
D	0030170	molecular_function	pyridoxal phosphate 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. FVaDEVic.GFgRtGewfgsdyydlkp....DLMtiAKgltSG

Chain	Residue	Details
A	PHE257-GLY294

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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":"P53555","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P12995","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	4
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"UniProtKB","id":"P53555","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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