Structure of PDB 4h6q Chain A

Receptor sequence
>4h6qA (length=281) Species: 243230 (Deinococcus radiodurans R1 = ATCC 13939 = DSM 20539) [Search protein sequence]
PQVEQLARQKMWNLAERFVAGESIESAIQAVQALERDGIAGNLDLLGEFI
DSPAKCTEFADDVIKLIEAAHAAGIKPYVSIKLSSVGQGKDENGEDLGLT
NARRIIAKAKEYGGFICLDMEDHTRVDVTLEQFRTLVGEFGAEHVGTVLQ
SYLYRSLGDRASLDDLRPNIRMVKGAYLEPATVAYPDKADVDQNYRRLVF
QHLKAGNYTNVATHDERIIDDVKRFVLAHGIGKDAFEFQMLYGIRRDLQK
QLAAEGYRVRVYLPYGRDWYAYFSRRIAETP
3D structure
PDB4h6q Crystal structures and kinetics of monofunctional proline dehydrogenase provide insight into substrate recognition and conformational changes associated with flavin reduction and product release.
ChainA
Resolution1.359 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.5.5.2: proline 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 FAD A D135 M136 Q166 R187 V189 K190 G191 A192 A228 T229 H230 M256 L257 I260 R292 E295 P297 D119 M120 Q150 R171 V173 K174 G175 A176 A212 T213 H214 M240 L241 I244 R276 E279 P281
BS02 TFB A K98 Y278 R291 R292 K82 Y262 R275 R276 MOAD: Ki=38mM
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004657 proline dehydrogenase activity
GO:0016491 oxidoreductase activity
GO:0071949 FAD binding
Biological Process
GO:0006560 proline metabolic process
GO:0006562 proline catabolic process
GO:0010133 proline catabolic process to glutamate

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Molecular Function
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Biological Process
External links
PDB RCSB:4h6q, PDBe:4h6q, PDBj:4h6q
PDBsum4h6q
PubMed23151026
UniProtQ9RW55|PRODH_DEIRA Proline dehydrogenase (Gene Name=DR_0814)

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