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7UT8

CryoEM structure of Azotobacter vinelandii nitrogenase complex (1:1 FeP:MoFeP, ATP-bound) during catalytic N2 reduction

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0009399biological_processnitrogen fixation
A0016163molecular_functionnitrogenase activity
A0016491molecular_functionoxidoreductase activity
A0016612cellular_componentmolybdenum-iron nitrogenase complex
A0018697molecular_functioncarbonyl sulfide nitrogenase activity
A0046872molecular_functionmetal ion binding
A0051536molecular_functioniron-sulfur cluster binding
B0005524molecular_functionATP binding
B0009399biological_processnitrogen fixation
B0016163molecular_functionnitrogenase activity
B0016491molecular_functionoxidoreductase activity
B0016612cellular_componentmolybdenum-iron nitrogenase complex
B0018697molecular_functioncarbonyl sulfide nitrogenase activity
B0046872molecular_functionmetal ion binding
B0051536molecular_functioniron-sulfur cluster binding
C0005524molecular_functionATP binding
C0009399biological_processnitrogen fixation
C0016163molecular_functionnitrogenase activity
C0016491molecular_functionoxidoreductase activity
C0016612cellular_componentmolybdenum-iron nitrogenase complex
C0018697molecular_functioncarbonyl sulfide nitrogenase activity
C0046872molecular_functionmetal ion binding
C0051536molecular_functioniron-sulfur cluster binding
D0005524molecular_functionATP binding
D0009399biological_processnitrogen fixation
D0016163molecular_functionnitrogenase activity
D0016491molecular_functionoxidoreductase activity
D0016612cellular_componentmolybdenum-iron nitrogenase complex
D0018697molecular_functioncarbonyl sulfide nitrogenase activity
D0046872molecular_functionmetal ion binding
D0051536molecular_functioniron-sulfur cluster binding
E0005524molecular_functionATP binding
E0009399biological_processnitrogen fixation
E0016163molecular_functionnitrogenase activity
E0016491molecular_functionoxidoreductase activity
E0018697molecular_functioncarbonyl sulfide nitrogenase activity
E0046872molecular_functionmetal ion binding
E0051539molecular_function4 iron, 4 sulfur cluster binding
F0005524molecular_functionATP binding
F0009399biological_processnitrogen fixation
F0016163molecular_functionnitrogenase activity
F0016491molecular_functionoxidoreductase activity
F0018697molecular_functioncarbonyl sulfide nitrogenase activity
F0046872molecular_functionmetal ion binding
F0051539molecular_function4 iron, 4 sulfur cluster binding
Functional Information from PROSITE/UniProt
site_idPS00692
Number of Residues14
DetailsNIFH_FRXC_2 NifH/frxC family signature 2. DvLGDVVCGGFAmP
ChainResidueDetails
EASP125-PRO138

site_idPS00746
Number of Residues13
DetailsNIFH_FRXC_1 NifH/frxC family signature 1. EsGGPepGvGCAG
ChainResidueDetails
EGLU87-GLY99

site_idPS00090
Number of Residues15
DetailsNITROGENASE_1_2 Nitrogenases component 1 alpha and beta subunits signature 2. TTCmaeviGDDLnAF
ChainResidueDetails
ASER152-VAL166
BTHR151-PHE165

site_idPS00699
Number of Residues8
DetailsNITROGENASE_1_1 Nitrogenases component 1 alpha and beta subunits signature 1. YVHGSQGC
ChainResidueDetails
AILE81-CYS88
BTYR88-CYS95

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING:
ChainResidueDetails
CCYS275
CHIS442
FGLY9
EGLY9
ECYS97
ECYS132
FCYS97
FCYS132
DCYS153
DSER188

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: ADP-ribosylarginine; by dinitrogenase reductase ADP-ribosyltransferase => ECO:0000250
ChainResidueDetails
EARG100
FARG100

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 212
ChainResidueDetails
ELYS10electrostatic stabiliser, hydrogen bond donor
ELYS15electrostatic stabiliser, hydrogen bond donor
ELYS41electrostatic stabiliser, hydrogen bond donor
EASP129hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

site_idMCSA2
Number of Residues4
DetailsM-CSA 212
ChainResidueDetails
FLYS10electrostatic stabiliser, hydrogen bond donor
FLYS15electrostatic stabiliser, hydrogen bond donor
FLYS41electrostatic stabiliser, hydrogen bond donor
FASP129hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

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PDB entries from 2024-06-12

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