2FZM

Structure of the E. coli PutA proline dehydrogenase domain reduced by dithionite and complexed with SO2

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003842	molecular_function	L-glutamate gamma-semialdehyde dehydrogenase (NAD+) activity
A	0004657	molecular_function	proline dehydrogenase activity
A	0006562	biological_process	L-proline catabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	31
Details	BINDING SITE FOR RESIDUE FAD A 2001

Chain	Residue
A	ASP370
A	ALA436
A	TYR437
A	TRP438
A	TYR456
A	THR457
A	ARG458
A	LYS459
A	THR462
A	ALA485
A	THR486
A	ALA371
A	HIS487
A	ASN488
A	GLN511
A	CYS512
A	LEU513
A	TYR540
A	GLU559
A	SER565
A	PHE566
A	HOH2021
A	VAL402
A	HOH2034
A	HOH2042
A	GLN404
A	TYR406
A	ARG431
A	VAL433
A	LYS434
A	GLY435

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site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO2 A 2002

Chain	Residue
A	LYS329
A	ALA436
A	ARG555
A	ARG556

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"evidences":[{"source":"UniProtKB","id":"Q72IB8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2006","submissionDatabase":"PDB data bank","title":"Hydrogen Bonding Interactions of the 2-OH Ribityl Group and the N(5) Position of the FAD Cofactor Regulate PutA-membrane Associations in Escherichia coli.","authors":["Zhang W.","Zhang M.","Zhu W.","Wanduragula S.","Rewinkel D.","Tanner J.J.","Becker D.F."]}},{"source":"PubMed","id":"12514740","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"15449943","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1TJ0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1TJ1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FZN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4O8A","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	17
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12514740","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15449943","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2006","submissionDatabase":"PDB data bank","title":"Hydrogen Bonding Interactions of the 2-OH Ribityl Group and the N(5) Position of the FAD Cofactor Regulate PutA-membrane Associations in Escherichia coli.","authors":["Zhang W.","Zhang M.","Zhu W.","Wanduragula S.","Rewinkel D.","Tanner J.J.","Becker D.F."]}},{"source":"PDB","id":"1TIW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1TJ0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1TJ1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1TJ2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FZN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4O8A","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2006","submissionDatabase":"PDB data bank","title":"Hydrogen Bonding Interactions of the 2-OH Ribityl Group and the N(5) Position of the FAD Cofactor Regulate PutA-membrane Associations in Escherichia coli.","authors":["Zhang W.","Zhang M.","Zhu W.","Wanduragula S.","Rewinkel D.","Tanner J.J.","Becker D.F."]}},{"source":"PDB","id":"2FZN","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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