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2Q4Z

Ensemble refinement of the protein crystal structure of an aspartoacylase from Rattus norvegicus

Functional Information from GO Data
ChainGOidnamespacecontents
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006083biological_processacetate metabolic process
A0006531biological_processaspartate metabolic process
A0016787molecular_functionhydrolase activity
A0016788molecular_functionhydrolase activity, acting on ester bonds
A0016811molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
A0019807molecular_functionaspartoacylase activity
A0022010biological_processcentral nervous system myelination
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A0048714biological_processpositive regulation of oligodendrocyte differentiation
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006083biological_processacetate metabolic process
B0006531biological_processaspartate metabolic process
B0016787molecular_functionhydrolase activity
B0016788molecular_functionhydrolase activity, acting on ester bonds
B0016811molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
B0019807molecular_functionaspartoacylase activity
B0022010biological_processcentral nervous system myelination
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
B0048714biological_processpositive regulation of oligodendrocyte differentiation
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 601
ChainResidue
AHIS20
AGLU23
AHIS115
AHOH748
AHOH778

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 701
ChainResidue
ATYR163
AHOH834
BARG308
BTHR310
AASP73
ALEU74
ALYS102
AASN103

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 702
ChainResidue
AARG196
ALYS199
AHIS200
AHOH962

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 703
ChainResidue
ATHR61
AHOH779
AHOH795
AHOH836
AHOH969
AHOH988
BTHR61

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 602
ChainResidue
BHIS20
BGLU23
BARG62
BHIS115
BHOH733

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 704
ChainResidue
BASP67
BASN69
BTYR287
BHOH878
BHOH927
BHOH943

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 705
ChainResidue
BARG196
BLYS199
BHIS200
BHOH763
BHOH922

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:P45381
ChainResidueDetails
AGLU177
BGLU177

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:17194761, ECO:0007744|PDB:2GU2
ChainResidueDetails
AHIS20
AGLU23
AHIS115
BHIS20
BGLU23
BHIS115

site_idSWS_FT_FI3
Number of Residues12
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P45381
ChainResidueDetails
AARG62
BARG167
BTYR287
AARG70
ATYR163
AARG167
ATYR287
BARG62
BASN69
BARG70
BTYR163
AASN69

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000250|UniProtKB:P45381
ChainResidueDetails
AARG62
BARG62

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PDB entries from 2024-05-29

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