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6Y72

Pseudomonas stutzeri nitrous oxide reductase mutant, H178A

Functional Information from GO Data
ChainGOidnamespacecontents
A0004129molecular_functioncytochrome-c oxidase activity
A0005507molecular_functioncopper ion binding
A0005509molecular_functioncalcium ion binding
A0016020cellular_componentmembrane
A0050304molecular_functionnitrous-oxide reductase activity
B0004129molecular_functioncytochrome-c oxidase activity
B0005507molecular_functioncopper ion binding
B0005509molecular_functioncalcium ion binding
B0016020cellular_componentmembrane
B0050304molecular_functionnitrous-oxide reductase activity
Functional Information from PDB Data
site_idAC1
Number of Residues11
Detailsbinding site for residue B3P A 701
ChainResidue
AARG114
BLYS122
BHOH956
AHIS590
AGLY591
ATHR605
AFMT708
AHOH808
AHOH836
AHOH869
AHOH918

site_idAC2
Number of Residues6
Detailsbinding site for residue NA A 702
ChainResidue
AMET168
AHOH979
AHOH1093
AHOH1128
AHOH1266
AHOH1304

site_idAC3
Number of Residues4
Detailsbinding site for residue NA A 703
ChainResidue
AASN173
AHOH1135
AHOH1367
AHOH1372

site_idAC4
Number of Residues6
Detailsbinding site for residue CA A 704
ChainResidue
ATYR256
AGLU259
AMET267
AASP273
AASN324
AHOH833

site_idAC5
Number of Residues4
Detailsbinding site for residue FMT A 705
ChainResidue
AHIS115
AGLY118
AHOH979
AHOH1234

site_idAC6
Number of Residues4
Detailsbinding site for residue FMT A 706
ChainResidue
AARG388
AASN390
ALYS403
AHOH854

site_idAC7
Number of Residues1
Detailsbinding site for residue FMT A 707
ChainResidue
AHOH1113

site_idAC8
Number of Residues6
Detailsbinding site for residue FMT A 708
ChainResidue
APHE606
AVAL607
AB3P701
AHOH808
AHOH882
AHOH1084

site_idAC9
Number of Residues6
Detailsbinding site for residue CL A 709
ChainResidue
AARG181
AASN241
AGLY327
ACYS328
AASN329
AHIS382

site_idAD1
Number of Residues6
Detailsbinding site for residue CUA A 710
ChainResidue
AHIS583
ACYS618
ATRP620
ACYS622
AHIS626
AMET629

site_idAD2
Number of Residues10
Detailsbinding site for residue B3P B 701
ChainResidue
ALYS122
AHOH999
BHIS590
BGLY591
BTHR605
BHOH838
BHOH924
BHOH933
BHOH1059
BHOH1123

site_idAD3
Number of Residues6
Detailsbinding site for residue CA B 702
ChainResidue
BTYR256
BGLU259
BMET267
BASP273
BASN324
BHOH840

site_idAD4
Number of Residues6
Detailsbinding site for residue K B 703
ChainResidue
AHOH829
AHOH920
BLYS454
BGLU469
BHOH817
BHOH992

site_idAD5
Number of Residues7
Detailsbinding site for residue FMT B 704
ChainResidue
ATRP615
BGLU196
BPHE197
BILE198
BASN238
BASN257
BHOH816

site_idAD6
Number of Residues2
Detailsbinding site for residue FMT B 705
ChainResidue
BASP511
BARG512

site_idAD7
Number of Residues3
Detailsbinding site for residue FMT B 706
ChainResidue
BMET135
BASP141
BTHR188

site_idAD8
Number of Residues6
Detailsbinding site for residue CUA B 707
ChainResidue
BHIS583
BCYS618
BTRP620
BCYS622
BHIS626
BMET629

Functional Information from PROSITE/UniProt
site_idPS00078
Number of Residues49
DetailsCOX2 CO II and nitrous oxide reductase dinuclear copper centers signature. VsHgfvvvnhgvsmeispqqtssitfvadkpglhwyy......CswfChalHmeM
ChainResidueDetails
AVAL581-MET629

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues40
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AHIS129
AHIS382
AHIS433
ALYS454
AGLU469
AHIS494
AHIS583
ACYS618
ATRP620
ACYS622
AHIS626
AHIS130
AMET629
BHIS129
BHIS130
BALA178
BTYR256
BGLU259
BMET267
BASP273
BASN324
BHIS326
AALA178
BHIS382
BHIS433
BLYS454
BGLU469
BHIS494
BHIS583
BCYS618
BTRP620
BCYS622
BHIS626
ATYR256
BMET629
AGLU259
AMET267
AASP273
AASN324
AHIS326

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PDB entries from 2024-07-17

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