Structure of PDB 6vjr Chain D

Receptor sequence
>6vjrD (length=500) Species: 436308 (Nitrosopumilus maritimus SCM1) [Search protein sequence]
TIRSGDDYIESLRGRDLKVYLFGELVKEPVDHPMIRPSINAVAETYDLAL
REEALASADSSITGLKVNRFLHIAESAEDLVLQNKMQRKLGQNTGTCFQR
CVGMDAMNSLHSTTFEIDEKHGTDYHKRFLEFVKMVQQENLVIGGAMTDP
KGDRSKGPSEQDDPDLFTRIVDTDEKGVYVSGAKAHQTGCINSHWIILMP
TIRLTESDKDWAIVGAIPADAKGVTYIYGRQSCDTRSMEEGDIDDGNAKF
GGQEALIILDRVFIPWDKVFMHGEYEFASMLVERFTCYHRRSYVCKTGLG
DVLIGAAATIADYNGVPKVSHIKDKIIEMTHLNETIFAAGIASSHQGQKM
KSGVYLNDDMLAQVCKHNVTRFPYEISRLAQDIAGGLVVTLPSEKDFRHP
EAGPLLKKYLAGRKGVDVENRMRILRLIENMTLGRNAVGYLTESMHGAGS
PQAQRIQIQRQMQVGYKKNLAKNLAGITNDVEEPKESSEYFKRVFKTKDS
3D structure
PDB6vjr Structural adaptation of oxygen tolerance in a key archaeal carbon fixation enzyme
ChainD
Resolution1.55 Å
3D
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
Enzyme Commision number 5.3.3.3: vinylacetyl-CoA Delta-isomerase.
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 D H327 D388 I389 G391 G392 H321 D382 I383 G385 G386
BS02 SF4 D C103 F104 C107 H295 Y299 C301 E449 C97 F98 C101 H289 Y293 C295 E443
BS03 FAD D M153 T154 K157 R160 H192 Q193 T194 E449 H452 S456 M147 T148 K151 R154 H186 Q187 T188 E443 H446 S450
BS04 FE D H295 Y299 E449 H289 Y293 E443
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0016491 oxidoreductase activity
GO:0016627 oxidoreductase activity, acting on the CH-CH group of donors
GO:0016853 isomerase activity
GO:0046872 metal ion binding
GO:0050393 vinylacetyl-CoA delta-isomerase activity
GO:0051539 4 iron, 4 sulfur cluster binding

View graph for
Molecular Function
External links
PDB RCSB:6vjr, PDBe:6vjr, PDBj:6vjr
PDBsum6vjr
PubMed
UniProtA9A1Y2

[Back to BioLiP]