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4H5U

Structural insights into yeast Nit2: wild-type yeast Nit2

Functional Information from GO Data
ChainGOidnamespacecontents
A0005575cellular_componentcellular_component
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0016787molecular_functionhydrolase activity
A0016811molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
A0043605biological_processamide catabolic process
A0050406molecular_function[acetyl-CoA carboxylase]-phosphatase activity
A0110050molecular_functiondeaminated glutathione amidase activity
B0005575cellular_componentcellular_component
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0016787molecular_functionhydrolase activity
B0016811molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
B0043605biological_processamide catabolic process
B0050406molecular_function[acetyl-CoA carboxylase]-phosphatase activity
B0110050molecular_functiondeaminated glutathione amidase activity
C0005575cellular_componentcellular_component
C0005737cellular_componentcytoplasm
C0005739cellular_componentmitochondrion
C0016787molecular_functionhydrolase activity
C0016811molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
C0043605biological_processamide catabolic process
C0050406molecular_function[acetyl-CoA carboxylase]-phosphatase activity
C0110050molecular_functiondeaminated glutathione amidase activity
D0005575cellular_componentcellular_component
D0005737cellular_componentcytoplasm
D0005739cellular_componentmitochondrion
D0016787molecular_functionhydrolase activity
D0016811molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
D0043605biological_processamide catabolic process
D0050406molecular_function[acetyl-CoA carboxylase]-phosphatase activity
D0110050molecular_functiondeaminated glutathione amidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 401
ChainResidue
AASP87
AASP116
ALEU122
AGOL403
AHOH579

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 402
ChainResidue
AHOH662
AHOH710
BARG58
BTYR59
AASP155
AILE156
AHOH573
AHOH604

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 403
ChainResidue
AHIS117
APRO160
AGOL401
AHOH558

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 404
ChainResidue
AARG182
AARG292
AASN293
APRO296
AHOH516
BGLU98
BLEU102

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL B 401
ChainResidue
AARG58
ATYR59
AHOH514
BASP155
BILE156
BHOH519
BHOH550
BHOH569

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 402
ChainResidue
AGLU98
BARG292
BASN293
BPRO296
BASN299
BGOL403
BHOH508

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 403
ChainResidue
AGLU98
AHOH519
BLYS163
BGLY185
BALA186
BARG292
BGOL402

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 404
ChainResidue
BARG209
BTRP262
BGLY263
BLYS264
BHOH577
BHOH700

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CAC B 405
ChainResidue
AHIS240
BILE68
BGLU124
BHOH553
BHOH599

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL C 401
ChainResidue
BARG7
BLEU280
BHOH618
CGLY226
CMET227
CHOH558

site_idBC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL C 402
ChainResidue
AALA202
AHIS203
CARG209
CTRP262
CGLY263
CLYS264
CHOH526
CHOH698

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL D 401
ChainResidue
DTHR196
DILE197
DLYS198
DARG249
DARG250
DGLU251

site_idBC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL D 402
ChainResidue
DARG209
DTRP262
DGLY263
DLYS264
DHOH550
DHOH648
DHOH649

site_idBC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL D 403
ChainResidue
DARG182
DGLN216
DARG292
DPRO296
DLEU297
DTRP298

Functional Information from PROSITE/UniProt
site_idPS01227
Number of Residues21
DetailsUPF0012 Uncharacterized protein family UPF0012 signature. GsaICYDIrFPefslklrsmG
ChainResidueDetails
AGLY165-GLY185

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00054
ChainResidueDetails
AGLU45
BGLU45
CGLU45
DGLU45

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU00054
ChainResidueDetails
ALYS127
BLYS127
CLYS127
DLYS127

site_idSWS_FT_FI3
Number of Residues4
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU00054, ECO:0000269|PubMed:23897470
ChainResidueDetails
ACAF169
BCAF169
CCAF169
DCAF169

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:23897470
ChainResidueDetails
AARG173
ATHR199
BARG173
BTHR199
CARG173
CTHR199
DARG173
DTHR199

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PDB entries from 2024-07-10

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