Structure of PDB 4nma Chain B

Receptor sequence
>4nmaB (length=979) Species: 243231 (Geobacter sulfurreducens PCA) [Search protein sequence]
SELNTKIVNRGKEFFGSISGEKPSLFNKGAWMGKAMDWSMQNEQFKIQMF
RFVDVFPSLTTSKLLTEHIREYFGNEQDMPAFMAVLNKVLTSNIEEMARQ
FIVGETTKEAVKNLEKLRKDGFAAVVDVLGEATLSEEEAEVYTNTYLELL
EALKKEQGSWKGLPGKGGDPGLDWGHAPKVNIAVKPTALFCLANPQDFEG
SVVAILDRMRRIFKKVMELNGFLCIDMESYRHKEIILEVFRRLKLEYRDY
PHLGIVLQAYLKDNDKDLDDLLAWAKEHKVQISVRLVKGAYWDYETVKAK
QNDWEVPVWTIKAESDAAYERQARKILENHQICHFACASHNIRTISAVME
MARELNVPEDRYEFQVLYGMAEPVRKGILKVAGRIRLYAPYGNMVPGMGY
LVRRLLENTANESFLRQSFAEDAQIERLLEDPAVTVERERAARAAKGLGG
LPPFNNEAMVDFTRADHRAAFPKHIAQVRTQLGKTYPLFINGKEVRTNDL
IPTVNPNKPSEVLGQICQAGTTEVGDAIAAAKAAFPAWRDTDPRTRAEYL
LKAAQAARKRLFELSAWQVLEIGKQWDQAYADVTEAIDFLEYYAREMIRL
GQPQRVGHAPGELNHYFYEPKGVAAVIAPWNFPLAISMGMASAAIVTGNC
VVFKPSGITSIIGWHLVELFREAGLPEGVFNFTPGRGSVMGDYLVDHPDI
SLIAFTGSMETGLRIIERAAKVHPGQANVKKIISEMGGKNAIIIDDDADL
DEAVPHVLYSAFGFQGQKCSACSRVIVLDAVYDKFIERLVSMAKATKVGP
SEDPANYMGAVADDKAMKSIKEYAEIGKREGHVLYESPVPAGEGYFVPMT
IIGGIKPEHRIAQEEIFGPVLAVMRAKDFDQAIEWANSTQFALTGGIFSR
SPEHLAKARREFRVGNLYINRNNTGALVERQPFGGARMSGVGTKAGGPDY
LLHFMDPRVVTENTMRRGFAPIEEDDDWV
3D structure
PDB4nma Structures of the PutA peripheral membrane flavoenzyme reveal a dynamic substrate-channeling tunnel and the quinone-binding site.
ChainB
Resolution2.101 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) N655 K678 E759 C793 E889 A969
Catalytic site (residue number reindexed from 1) N631 K654 E735 C769 E865 A945
Enzyme Commision number 1.2.1.88: L-glutamate gamma-semialdehyde dehydrogenase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003700 DNA-binding transcription factor activity
GO:0003842 1-pyrroline-5-carboxylate dehydrogenase activity
GO:0004657 proline dehydrogenase activity
GO:0016491 oxidoreductase activity
GO:0016620 oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
Biological Process
GO:0006355 regulation of DNA-templated transcription
GO:0006562 proline catabolic process
GO:0010133 proline catabolic process to glutamate
Cellular Component
GO:0005737 cytoplasm
GO:0009898 cytoplasmic side of plasma membrane

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4nma, PDBe:4nma, PDBj:4nma
PDBsum4nma
PubMed24550478
UniProtQ746X3

[Back to BioLiP]