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3VLZ

Assimilatory nitrite reductase (Nii3) - N226K mutant - SO3 full complex from tobacco leaf

Functional Information from GO Data
ChainGOidnamespacecontents
A0016491molecular_functionoxidoreductase activity
A0020037molecular_functionheme binding
A0042128biological_processnitrate assimilation
A0046872molecular_functionmetal ion binding
A0048307molecular_functionferredoxin-nitrite reductase activity
A0051536molecular_functioniron-sulfur cluster binding
A0051539molecular_function4 iron, 4 sulfur cluster binding
Functional Information from PDB Data
site_idAC1
Number of Residues36
DetailsBINDING SITE FOR RESIDUE SRM A 601
ChainResidue
AARG98
ALYS224
ALYS226
APHE264
APHE265
ASER266
AARG309
AGLN402
ACYS440
ATHR441
ACYS446
AARG109
AASN483
ATHR484
ACYS485
AGLN487
ASO3606
AHOH1004
AHOH1005
AHOH1022
AHOH1039
AHOH1040
ATHR141
AHOH1060
AHOH1087
AHOH1127
AHOH1174
AHOH1251
AHOH1291
AHOH1378
ATHR142
AARG143
AASN145
AGLN147
AARG149
AARG223

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SF4 A 602
ChainResidue
ACYS440
ACYS446
AALA449
ATHR479
AGLY480
ACYS481
AASN483
ACYS485

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K A 603
ChainResidue
AILE371
AGLU401
AGLN402
AASN403
AHOH1013
AHOH1027

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 604
ChainResidue
AMET175
AHOH1251

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 605
ChainResidue
AARG99
ALYS100

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO3 A 606
ChainResidue
AARG109
AARG179
ALYS224
ALYS226
ASRM601
AHOH1022

Functional Information from PROSITE/UniProt
site_idPS00365
Number of Residues17
DetailsNIR_SIR Nitrite and sulfite reductases iron-sulfur/siroheme-binding site. TGCpntCaqvqvaDIGF
ChainResidueDetails
ATHR479-PHE495

222624

PDB entries from 2024-07-17

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