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1MZZ

Crystal Structure of Mutant (M182T)of Nitrite Reductase

Functional Information from GO Data
ChainGOidnamespacecontents
A0005507molecular_functioncopper ion binding
A0016491molecular_functionoxidoreductase activity
A0019333biological_processdenitrification pathway
A0042128biological_processnitrate assimilation
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
A0050421molecular_functionnitrite reductase (NO-forming) activity
B0005507molecular_functioncopper ion binding
B0016491molecular_functionoxidoreductase activity
B0019333biological_processdenitrification pathway
B0042128biological_processnitrate assimilation
B0042597cellular_componentperiplasmic space
B0046872molecular_functionmetal ion binding
B0050421molecular_functionnitrite reductase (NO-forming) activity
C0005507molecular_functioncopper ion binding
C0016491molecular_functionoxidoreductase activity
C0019333biological_processdenitrification pathway
C0042128biological_processnitrate assimilation
C0042597cellular_componentperiplasmic space
C0046872molecular_functionmetal ion binding
C0050421molecular_functionnitrite reductase (NO-forming) activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU A 401
ChainResidue
AHIS126
ACYS167
AHIS177
ATHR182

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CU A 402
ChainResidue
AASP129
AHIS131
AHIS166
AHOH3541
BHIS1338

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU B 1401
ChainResidue
BHIS1126
BCYS1167
BHIS1177
BTHR1182

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU B 1402
ChainResidue
BHIS1131
BHIS1166
BHOH3542
CHIS2338

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU C 2401
ChainResidue
CHIS2126
CCYS2167
CHIS2177
CTHR2182

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CU C 2402
ChainResidue
AHIS338
CASP2129
CHIS2131
CHIS2166
CHOH3543

Functional Information from PROSITE/UniProt
site_idPS00283
Number of Residues17
DetailsSOYBEAN_KUNITZ Soybean trypsin inhibitor (Kunitz) protease inhibitors family signature. LkDHEGKpVrYDtvYyI
ChainResidueDetails
ALEU194-ILE210

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues288
DetailsDomain: {"description":"Plastocyanin-like 1"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues303
DetailsDomain: {"description":"Plastocyanin-like 2"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues12
DetailsBinding site: {"description":"type 1 copper site","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues9
DetailsBinding site: {"description":"type 2 copper site","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1nid
ChainResidueDetails
AGLY97
APHE95

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1nid
ChainResidueDetails
BPHE1095
BGLY1097

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1nid
ChainResidueDetails
CGLY2097
CPHE2095

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1nid
ChainResidueDetails
AHIS287
AASP129

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1nid
ChainResidueDetails
BHIS1287
BASP1129

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1nid
ChainResidueDetails
CASP2129
CHIS2287

239803

PDB entries from 2025-08-06

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