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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 A1479
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 B1479
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: BINDING => ECO:0000269|PubMed:15772287, ECO:0007744|PDB:2BII
ChainResidueDetails
ACYS139
BCYS139

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 2024-07-24

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