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1N15

FOLLOWING THE C HEME REDUCTION IN 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 Residues15
DetailsBINDING SITE FOR RESIDUE HEC A 601
ChainResidue
AHIS51
ATHR59
ALEU63
AARG71
ALEU79
AILE80
ATHR84
ALEU86
AGLY87
AMET88
ATRP91
BGLU8
AARG46
ACYS47
ACYS50

site_idAC2
Number of Residues20
DetailsBINDING SITE FOR RESIDUE DHE A 602
ChainResidue
AARG156
AHIS182
AILE183
AARG185
AARG198
AARG225
ASER226
ATYR245
AALA283
AALA284
AILE285
AHIS327
AARG372
APHE425
APHE441
AGLN483
AGLY531
APHE533
BTYR10
BALA13

site_idAC3
Number of Residues14
DetailsBINDING SITE FOR RESIDUE HEC B 601
ChainResidue
BARG46
BCYS47
BCYS50
BHIS51
BTHR59
BLEU63
BARG71
BLEU79
BTHR84
BLEU86
BGLY87
BMET88
BPRO89
BTRP91

site_idAC4
Number of Residues19
DetailsBINDING SITE FOR RESIDUE DHE B 602
ChainResidue
ATYR10
AALA13
BARG156
BHIS182
BARG185
BARG198
BARG225
BSER226
BTYR245
BALA283
BALA284
BILE285
BHIS327
BARG372
BPHE425
BGLN483
BTRP498
BGLY531
BPHE533

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_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

218853

PDB entries from 2024-04-24

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