Structure of PDB 1mio Chain A

Receptor sequence
>1mioA (length=525) Species: 1501 (Clostridium pasteurianum) [Search protein sequence]
SENLKDEILEKYIPKTKKTRSGHIVIKTEETPNPEIVANTRTVPGIITAR
GCAYAGCKGVVMGPIKDMVHITHGPIGCSFYTWGGRRFKSKPENGTGLNF
NEYVFSTDMQESDIVFGGVNKLKDAIHEAYEMFHPAAIGVYATCPVGLIG
DDILAVAATASKEIGIPVHAFSCEGYKGVSQSAGHHIANNTVMTDIIGKG
NKEQKKYSINVLGEYNIGGDAWEMDRVLEKIGYHVNATLTGDATYEKVQN
ADKADLNLVQCHRSINYIAEMMETKYGIPWIKCNFIGVDGIVETLRDMAK
CFDDPELTKRTEEVIAEEIAAIQDDLDYFKEKLQGKTACLYVGGSRSHTY
MNMLKSFGVDSLVAGFEFAHRDDYEGREVIPTIKIDADSKNIPEITVTPD
EQKYRVVIPEDKVEELKKAGVPLSSYGGMMKEMHDGTILIDDMNHHDMEV
VLEKLKPDMFFAGIKEKFVIQKGGVLSKQLHSYDYNGPYAGFRGVVNFGH
ELVNGIYTPAWKMITPPWKKASSES
3D structure
PDB1mio X-ray crystal structure of the nitrogenase molybdenum-iron protein from Clostridium pasteurianum at 3.0-A resolution.
ChainA
Resolution3.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C53 A56 R87 H186
Catalytic site (residue number reindexed from 1) C52 A55 R86 H185
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 CFM A V61 R87 H186 Y216 C262 S265 G344 G345 S346 R347 F369 H482 V60 R86 H185 Y215 C261 S264 G343 G344 S345 R346 F368 H481
BS02 CLP A C53 Y55 P76 G78 C79 C145 G176 C52 Y54 P75 G77 C78 C144 G175
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:1mio, PDBe:1mio, PDBj:1mio
PDBsum1mio
PubMed8393705
UniProtP00467|NIFD_CLOPA Nitrogenase molybdenum-iron protein alpha chain (Gene Name=nifD)

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