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1GJQ

Pseudomonas aeruginosa cd1 nitrite reductase reduced cyanide complex

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 CYN A 603
ChainResidue
AHIS327
AHIS369
ADHE602
BTYR10

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CYN B 603
ChainResidue
ATYR10
BHIS327
BHIS369
BDHE602

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE HEC A 601
ChainResidue
ACYS47
ACYS50
AHIS51
ATHR59
AGLY60
ALYS61
ALEU63
AARG71
ALEU79
ATHR84
ALEU86
AGLY87
AMET88
ATRP91
AARG46

site_idAC4
Number of Residues28
DetailsBINDING SITE FOR RESIDUE DHE A 602
ChainResidue
AARG156
AHIS182
AARG185
AARG198
AARG225
ASER226
ATYR245
AALA284
AILE285
AHIS327
AARG372
APHE425
APHE441
AGLN483
AGLY531
APHE533
ACYN603
AHOH2103
AHOH2107
AHOH2124
AHOH2185
AHOH2209
AHOH2282
AHOH2283
AHOH2284
AHOH2285
BTYR10
BHOH2009

site_idAC5
Number of Residues16
DetailsBINDING SITE FOR RESIDUE HEC B 601
ChainResidue
BARG46
BCYS47
BCYS50
BHIS51
BTHR59
BGLY60
BLYS61
BLEU63
BARG71
BLEU79
BTHR84
BLEU86
BGLY87
BMET88
BTRP91
BHOH2308

site_idAC6
Number of Residues28
DetailsBINDING SITE FOR RESIDUE DHE B 602
ChainResidue
ATYR10
AALA13
BARG156
BHIS182
BILE183
BARG185
BARG198
BARG225
BSER226
BTYR245
BALA284
BILE285
BHIS327
BARG372
BPHE425
BPHE441
BGLN483
BGLY531
BPHE533
BCYN603
BHOH2120
BHOH2122
BHOH2124
BHOH2310
BHOH2311
BHOH2312
BHOH2313
BHOH2314

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
DetailsAnnotated By Reference To The Literature 1nir
ChainResidueDetails
AHIS369
AHIS327

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1nir
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 2024-09-18

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