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2BII

crystal structure of nitrate-reducing fragment of assimilatory nitrate reductase from Pichia angusta

Functional Information from GO Data
ChainGOidnamespacecontents
A0016491molecular_functionoxidoreductase activity
A0030151molecular_functionmolybdenum ion binding
A0043546molecular_functionmolybdopterin cofactor binding
B0016491molecular_functionoxidoreductase activity
B0030151molecular_functionmolybdenum ion binding
B0043546molecular_functionmolybdopterin cofactor binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 601
ChainResidue
ALYS145
AASN157
AASN453
AHOH2383

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 602
ChainResidue
APHE156
AHOH2385
AHOH2386
APRO64
AASN66
AARG89
AARG144
AGLY155

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 603
ChainResidue
AARG295
AGLY338
AARG339
AASP410

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 B 601
ChainResidue
BPRO64
BASN66
BARG89
BGLY155
BPHE156
BHOH2386
BHOH2387
BHOH2388

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 602
ChainResidue
BLYS145
BASN157
BASN453
BLYS454
BHOH2389

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA B 603
ChainResidue
BARG295
BARG339
BMET409
BASP410
BMET413

site_idAC7
Number of Residues22
DetailsBINDING SITE FOR RESIDUE MTV A 1479
ChainResidue
AHIS86
APHE87
AVAL88
AARG89
AHIS91
AMET137
ACYS139
AALA140
AASP195
ATYR202
AHIS233
AARG238
AILE245
AGLY246
AGLY247
ASER249
AVAL250
ALYS251
ATRP252
AASN272
AHOH2395
AHOH2396

site_idAC8
Number of Residues21
DetailsBINDING SITE FOR RESIDUE MTV B 1479
ChainResidue
BHIS86
BPHE87
BVAL88
BARG89
BHIS91
BMET137
BCYS139
BALA140
BASP195
BTYR202
BHIS233
BARG238
BGLY246
BGLY247
BSER249
BVAL250
BLYS251
BTRP252
BASN272
BHOH2186
BHOH2399

site_idAC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 701
ChainResidue
ALYS402
AARG434
AILE437
AILE438
AGLU476
AHOH2381
AHOH2388
AHOH2389

site_idBC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 702
ChainResidue
AALA160
AASN312
AVAL450
AVAL451
AALA452
AHOH2390
AHOH2391
AHOH2392

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 703
ChainResidue
ASER67
APRO69
ASER84
ALEU85
AHIS86
AHOH2393

site_idBC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL B 701
ChainResidue
BLYS402
BARG434
BILE437
BILE438
BGLU476
BHOH2382
BHOH2391
BHOH2392

site_idBC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL B 702
ChainResidue
BGLY159
BALA160
BASN312
BVAL450
BVAL451
BALA452
BHOH2394
BHOH2396

site_idBC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 703
ChainResidue
BGLY111
BTRP190
BVAL257
BVAL258
BSER259
BARG261
BHOH2398

site_idBC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 704
ChainResidue
BSER67
BPRO69
BPRO70
BLEU85
BHIS86
BHOH2008

Functional Information from PROSITE/UniProt
site_idPS00559
Number of Residues36
DetailsMOLYBDOPTERIN_EUK Eukaryotic molybdopterin oxidoreductases signature. GMveTpykiklsdimeq..FdiySTpvtMvCagNRrkE
ChainResidueDetails
AGLY111-GLU146

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15772287","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2BII","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 925
ChainResidueDetails
ACYS139metal ligand
AASP271electrostatic stabiliser, transition state stabiliser
AASN272electrostatic stabiliser, transition state stabiliser

site_idMCSA2
Number of Residues3
DetailsM-CSA 925
ChainResidueDetails
BCYS139metal ligand
BASP271electrostatic stabiliser, transition state stabiliser
BASN272electrostatic stabiliser, transition state stabiliser

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PDB entries from 2026-09-30

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