Structure of PDB 5koh Chain D

Receptor sequence
>5kohD (length=510) Species: 272568 (Gluconacetobacter diazotrophicus PA1 5) [Search protein sequence]
PQNVDKILDHAPLFREPEYQEMLAGKAKLENMPPADKVVEIADWTKSWEY
REKNFARESLSVNPAKACQPLGAVFVASGFERTMSFVHGSQGCVAYYRSH
LSRHFKEPSSAVSSSMTEDAAVFGGLNNMVDGLANTYKLYDPKMIAVSTT
CMAEVIGDDLHAFIQTAKGKGSVPEEFDVPFAHTPAFVGSHVTGYDNMLK
GILEHFWKGRTPVPNRSVNIIPGFDGFAVGNNRELKRILGMMGVQYTILS
DVSDQFDTPSDGEYRMYDGGTKIEAARDAVNADYTISLQEYCTPKTLEYC
QSFGQKTASFHYPLGIGATDDLLQKLSEISGKPVPQELEMERGRLVDALA
DSQAYLHGKTYAIYGDPDFVYGMARFILETGGEPKHCLATNGSKAWEAQM
QELFDSSPFGVGCKAWGGKDLWHMRSLLATEKVDLLIGNSYGKYLERDTD
TPLIRLMFPIFDRHHHHRFPVWGYQGALRVLVTLLDKIFDKLDDDTIQAG
VTDYSFDLTR
3D structure
PDB5koh Tyrosine-Coordinated P-Cluster in G. diazotrophicus Nitrogenase: Evidence for the Importance of O-Based Ligands in Conformationally Gated Electron Transfer.
ChainD
Resolution1.83 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C152 V156
Catalytic site (residue number reindexed from 1) C151 V155
Enzyme Commision number 1.18.6.1: nitrogenase.
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 FE D K107 E108 K106 E107
BS02 FE D D348 D352 D347 D351
BS03 CLF D C69 G93 C94 Y97 Y98 T151 C152 A187 C68 G92 C93 Y96 Y97 T150 C151 A186
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016163 nitrogenase activity
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
GO:0051536 iron-sulfur cluster binding
Biological Process
GO:0009399 nitrogen fixation
Cellular Component
GO:0016612 molybdenum-iron nitrogenase complex

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:5koh, PDBe:5koh, PDBj:5koh
PDBsum5koh
PubMed27487256
UniProtA9H5W8

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