Structure of PDB 1qgu Chain B

Receptor sequence
>1qguB (length=519) Species: 573 (Klebsiella pneumoniae) [Search protein sequence]
SQTIDKINSCYPLFEQDEYQELFRNKRQLEEAHDAQRVQEVFAWTTTAEY
EALNFRREALTVDPAKACQPLGAVLCSLGFANTLPYVHGSQGCVAYFRTY
FNRHFKEPIACVSDSMTEDAAVFGGNNNMNLGLQNASALYKPEIIAVSTT
CMAEVIGDDLQAFIANAKKDGFVDSSIAVPHAHTPSFIGSHVTGWDNMFE
GFAKTFTADYQGQPGKLPKLNLVTGFETYLGNFRVLKRMMEQMAVPCSLL
SDPSEVLDTPADGHYRMYSGGTTQQEMKEAPDAIDTLLLQPWQLLKSKKV
VQEMWNQPATEVAIPLGLAATDELLMTVSQLSGKPIADALTLERGRLVDM
MLDSHTWLHGKKFGLYGDPDFVMGLTRFLLELGCEPTVILSHNANKRWQK
AMNKMLDASPYGRDSEVFINCDLWHFRSLMFTRQPDFMIGNSYGKFIQRD
TLAKGKAFEVPLIRLGFPLFDRHHLHRQTTWGYEGAMNIVTTLVNAVLEK
LDSDTSQLGKTDYSFDLVR
3D structure
PDB1qgu New insights into structure-function relationships in nitrogenase: A 1.6 A resolution X-ray crystallographic study of Klebsiella pneumoniae MoFe-protein.
ChainB
Resolution1.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C151 V155
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 CLF B C68 S90 G92 C93 Y96 T150 C151 S186 C68 S90 G92 C93 Y96 T150 C151 S186
BS02 MG B D349 D353 D349 D353
BS03 MG B K106 E107 K106 E107
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:1qgu, PDBe:1qgu, PDBj:1qgu
PDBsum1qgu
PubMed10525412
UniProtP09772|NIFK_KLEPN Nitrogenase molybdenum-iron protein beta chain (Gene Name=nifK)

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