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1NIR

OXYDIZED NITRITE REDUCTASE FROM PSEUDOMONAS AERUGINOSA

Functional Information from GO Data
ChainGOidnamespacecontents
A0009055molecular_functionelectron transfer activity
A0016491molecular_functionoxidoreductase activity
A0020037molecular_functionheme binding
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
A0050418molecular_functionhydroxylamine reductase activity
A0050421molecular_functionnitrite reductase (NO-forming) activity
B0009055molecular_functionelectron transfer activity
B0016491molecular_functionoxidoreductase activity
B0020037molecular_functionheme binding
B0042597cellular_componentperiplasmic space
B0046872molecular_functionmetal ion binding
B0050418molecular_functionhydroxylamine reductase activity
B0050421molecular_functionnitrite reductase (NO-forming) activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 A 604
ChainResidue
BHOH770
AHOH673
BHIS335
BHIS540

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 605
ChainResidue
ASER265
BGLY268
BMET269

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE OH A 603
ChainResidue
AHIS369
ADHE602
BTYR10

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 B 604
ChainResidue
AHIS335
AHIS540
AHOH744
BHOH984

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 605
ChainResidue
AGLY268
AMET269
BSER265

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE OH B 603
ChainResidue
ATYR10
BHIS369
BDHE602

site_idAC7
Number of Residues19
DetailsBINDING SITE FOR RESIDUE HEC A 601
ChainResidue
AARG46
ACYS47
ACYS50
AHIS51
ATHR59
ALEU63
AARG71
ALEU79
ATHR84
ALEU86
AGLY87
AMET88
APRO89
ATRP91
AHOH722
AHOH770
AHOH822
AHOH895
BGLU8

site_idAC8
Number of Residues29
DetailsBINDING SITE FOR RESIDUE DHE A 602
ChainResidue
AARG156
AHIS182
AILE183
AARG185
AARG198
AARG225
ASER226
ATYR245
AALA283
AALA284
AILE285
AHIS327
AARG372
APHE425
AGLN483
AGLY531
APHE533
AOH603
AHOH645
AHOH656
AHOH876
AHOH877
AHOH880
AHOH901
AHOH907
AHOH1010
BTYR10
BALA13
BHOH884

site_idAC9
Number of Residues19
DetailsBINDING SITE FOR RESIDUE HEC B 601
ChainResidue
AGLU8
BARG46
BCYS47
BCYS50
BHIS51
BTHR59
BLEU63
BARG71
BLEU79
BTHR84
BLEU86
BGLY87
BMET88
BPRO89
BTRP91
BHOH639
BHOH682
BHOH725
BHOH849

site_idBC1
Number of Residues28
DetailsBINDING SITE FOR RESIDUE DHE B 602
ChainResidue
BSER226
BTYR245
BALA284
BILE285
BHIS327
BARG372
BPHE425
BPHE441
BGLN483
BGLY531
BPHE533
BOH603
BHOH609
BHOH640
BHOH662
BHOH711
BHOH863
BHOH872
BHOH890
BHOH891
BHOH980
BHOH981
ATYR10
BARG156
BHIS182
BARG185
BARG198
BARG225

site_idNIA
Number of Residues3
DetailsACTIVE SITE.
ChainResidue
AHIS327
AHIS369
ADHE602

site_idNIB
Number of Residues3
DetailsACTIVE SITE.
ChainResidue
BHIS327
BHIS369
BDHE602

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: covalent => ECO:0000269|PubMed:9331415, ECO:0007744|PDB:1NIR
ChainResidueDetails
ACYS47
ACYS50
BCYS47
BCYS50

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:9331415, ECO:0007744|PDB:1NIR
ChainResidueDetails
AHIS51
AMET88
BHIS51
BMET88

site_idSWS_FT_FI3
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:9331415, ECO:0007744|PDB:1NIR
ChainResidueDetails
AARG71
BARG225
BSER226
BTYR245
BARG372
BGLN483
ATHR84
AARG225
ASER226
ATYR245
AARG372
AGLN483
BARG71
BTHR84

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: proximal binding residue => ECO:0000269|PubMed:9331415, ECO:0007744|PDB:1NIR
ChainResidueDetails
AHIS182
BHIS182

Catalytic Information from CSA
site_idCSA1
Number of Residues2
Detailsa catalytic site defined by CSA, PubMed 11226222
ChainResidueDetails
AHIS369
AHIS327

site_idCSA2
Number of Residues2
Detailsa catalytic site defined by CSA, PubMed 11226222
ChainResidueDetails
BHIS369
BHIS327

site_idMCSA1
Number of Residues6
DetailsM-CSA 903
ChainResidueDetails
ACYS47covalently attached
ACYS50covalently attached
AHIS51metal ligand
AMET88metal ligand
AHIS327electrostatic stabiliser
AHIS369electrostatic stabiliser

site_idMCSA2
Number of Residues6
DetailsM-CSA 903
ChainResidueDetails
BCYS47covalently attached
BCYS50covalently attached
BHIS51metal ligand
BMET88metal ligand
BHIS327electrostatic stabiliser
BHIS369electrostatic stabiliser

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PDB entries from 2024-07-31

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