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5OF7

Cu nitrite reductase serial data at varying temperatures 190K 0.48MGy

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
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue CU A 401
ChainResidue
AHIS95
ACYS136
AHIS145
AMET150

site_idAC2
Number of Residues5
Detailsbinding site for residue CU A 402
ChainResidue
AHIS100
AHIS135
AHIS306
ANO2406
ANO416

site_idAC3
Number of Residues6
Detailsbinding site for residue SO4 A 403
ChainResidue
APRO158
AARG159
AASP160
AHOH513
AHOH524
AHOH602

site_idAC4
Number of Residues7
Detailsbinding site for residue NO2 A 404
ChainResidue
AVAL68
APRO69
AASN151
AGLY179
AGLU180
AGLN181
AHOH542

site_idAC5
Number of Residues4
Detailsbinding site for residue NO2 A 405
ChainResidue
AVAL335
ALYS336
AHOH570
AHOH611

site_idAC6
Number of Residues8
Detailsbinding site for residue NO2 A 406
ChainResidue
AASP98
AHIS100
AHIS135
AHIS255
AILE257
AHIS306
ACU402
ANO416

site_idAC7
Number of Residues6
Detailsbinding site for residue ACT A 407
ChainResidue
APHE24
ALYS174
ATYR176
ATHR234
AHOH506
AHOH546

site_idAC8
Number of Residues7
Detailsbinding site for residue ACT A 408
ChainResidue
ATRP265
ATHR267
AGLY268
ALYS269
AASN272
AGLN278
AHOH512

site_idAC9
Number of Residues1
Detailsbinding site for residue SO4 A 409
ChainResidue
AARG123

site_idAD1
Number of Residues6
Detailsbinding site for residue SO4 A 410
ChainResidue
ALYS125
ATHR127
AARG296
ALEU330
AHOH577
AHOH628

site_idAD2
Number of Residues6
Detailsbinding site for residue SO4 A 411
ChainResidue
ALYS33
AASP188
AGLU189
ALYS194
AHOH756
AHOH807

site_idAD3
Number of Residues5
Detailsbinding site for residue SO4 A 412
ChainResidue
ATHR228
AGLY229
AHIS319
ALYS321
AHOH509

site_idAD4
Number of Residues6
Detailsbinding site for residue MLI A 413
ChainResidue
AGLY225
AHIS319
AHOH511
AHOH532
AHOH583
AHOH661

site_idAD5
Number of Residues7
Detailsbinding site for residue NO2 A 414
ChainResidue
AARG211
ATHR216
AHIS217
AVAL224
ALEU314
AHOH719
AHOH743

site_idAD6
Number of Residues2
Detailsbinding site for residue NO A 415
ChainResidue
APRO88
AASP89

site_idAD7
Number of Residues7
Detailsbinding site for residue NO A 416
ChainResidue
AASP98
AHIS100
AHIS135
AILE257
AHIS306
ACU402
ANO2406

site_idAD8
Number of Residues6
Detailsbinding site for residue NO A 417
ChainResidue
ALEU93
ALEU94
AMET141
AGLY324
AGLU325
AHOH534

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: type 1 copper site
ChainResidueDetails
AHIS95
ACYS136
AHIS145
AMET150

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: type 2 copper site
ChainResidueDetails
AHIS100
AHIS135
AHIS306

Catalytic Information from CSA
site_idMCSA1
Number of Residues11
DetailsM-CSA 4
ChainResidueDetails
AHIS95metal ligand
ATHR280electrostatic stabiliser, modifies pKa
AHIS306metal ligand
AASP98activator, hydrogen bond acceptor, proton acceptor, proton donor
AHIS100metal ligand
AHIS135metal ligand, single electron acceptor, single electron donor, single electron relay
ACYS136metal ligand, single electron acceptor, single electron donor, single electron relay
AHIS145metal ligand
AMET150metal ligand
AHIS255hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AGLU279electrostatic stabiliser, modifies pKa

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PDB entries from 2024-07-31

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