Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1DE0

MODULATING THE MIDPOINT POTENTIAL OF THE [4FE-4S] CLUSTER OF THE NITROGENASE FE PROTEIN

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005524molecular_functionATP binding
A0009399biological_processnitrogen fixation
A0016163molecular_functionnitrogenase activity
A0016491molecular_functionoxidoreductase activity
A0018697molecular_functioncarbonyl sulfide nitrogenase activity
A0046872molecular_functionmetal ion binding
A0051536molecular_functioniron-sulfur cluster binding
A0051539molecular_function4 iron, 4 sulfur cluster binding
B0000166molecular_functionnucleotide binding
B0005524molecular_functionATP binding
B0009399biological_processnitrogen fixation
B0016163molecular_functionnitrogenase activity
B0016491molecular_functionoxidoreductase activity
B0018697molecular_functioncarbonyl sulfide nitrogenase activity
B0046872molecular_functionmetal ion binding
B0051536molecular_functioniron-sulfur cluster 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

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon