Structure of PDB 1mio Chain D

Receptor sequence
>1mioD (length=457) Species: 1501 (Clostridium pasteurianum) [Search protein sequence]
LDATPKEIVERKALRINPAKTCQPVGAMYAALGIHNCLPHSHGSQGCCSY
HRTVLSRHFKEPAMASTSSFTEGASVFGGGSNIKTAVKNIFSLYNPDIIA
VHTTCLSETLGDDLPTYISQMEDAGSIPEGKLVIHTNTPSYVGSHVTGFA
NMVQGIVNYLSENTGAKNGKINVIPGFVGPADMREIKRLFEAMDIPYIMF
PDTSGVLDGPTTGEYKMYPEGGTKIEDLKDTGNSDLTLSLGSYASDLGAK
TLEKKCKVPFKTLRTPIGVSATDEFIMALSEATGKEVPASIEEERGQLID
LMIDAQQYLQGKKVALLGDPDEIIALSKFIIELGAIPKYVVTGTPGMKFQ
KEIDAMLAEAGIEGSKVKVEGDFFDVHQWIKNEGVDLLISNTYGKFIARE
ENIPFVRFGFPIMDRYGHYYNPKVGYKGAIRLVEEITNVILDKIERECTE
EDFEVVR
3D structure
PDB1mio X-ray crystal structure of the nitrogenase molybdenum-iron protein from Clostridium pasteurianum at 3.0-A resolution.
ChainD
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) C106 T110
Catalytic site (residue number reindexed from 1) C105 T109
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 CA D D301 D305 D300 D304
BS02 CA D K61 E62 K60 E61
BS03 CLP D C23 P25 S45 G47 C48 Y51 H52 T105 C106 S141 C22 P24 S44 G46 C47 Y50 H51 T104 C105 S140
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
UniProtP11347|NIFK_CLOPA Nitrogenase molybdenum-iron protein beta chain (Gene Name=nifK)

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