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1XDB

Crystal Structure of the Nitrogenase Fe protein Asp129Glu

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0009399biological_processnitrogen fixation
A0016163molecular_functionnitrogenase activity
A0016491molecular_functionoxidoreductase activity
A0018697molecular_functioncarbonyl sulfide nitrogenase activity
A0046872molecular_functionmetal ion binding
A0051539molecular_function4 iron, 4 sulfur cluster binding
B0005524molecular_functionATP binding
B0009399biological_processnitrogen fixation
B0016163molecular_functionnitrogenase activity
B0016491molecular_functionoxidoreductase activity
B0018697molecular_functioncarbonyl sulfide nitrogenase activity
B0046872molecular_functionmetal ion binding
B0051539molecular_function4 iron, 4 sulfur cluster binding
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SF4 A 290
ChainResidue
ACYS97
AALA98
ACYS132
AGLY134
BCYS97
BALA98
BCYS132
BGLY134

Functional Information from PROSITE/UniProt
site_idPS00746
Number of Residues13
DetailsNIFH_FRXC_1 NifH/frxC family signature 1. EsGGPepGvGCAG
ChainResidueDetails
AGLU87-GLY99

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING:
ChainResidueDetails
ALYS10
AALA98
AGLY133
BLYS10
BALA98
BGLY133

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: ADP-ribosylarginine; by dinitrogenase reductase ADP-ribosyltransferase => ECO:0000250
ChainResidueDetails
AGLY101
BGLY101

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 212
ChainResidueDetails
AGLY11electrostatic stabiliser, hydrogen bond donor
ASER16electrostatic stabiliser, hydrogen bond donor
AALA42electrostatic stabiliser, hydrogen bond donor
AVAL130hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

site_idMCSA2
Number of Residues4
DetailsM-CSA 212
ChainResidueDetails
BGLY11electrostatic stabiliser, hydrogen bond donor
BSER16electrostatic stabiliser, hydrogen bond donor
BALA42electrostatic stabiliser, hydrogen bond donor
BVAL130hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1f48
ChainResidueDetails
ALYS15
AGLY12

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1f48
ChainResidueDetails
BLYS15
BGLY12

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PDB entries from 2024-05-01

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