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3NH4

Crystal structure of murine aminoacylase 3

Functional Information from GO Data
ChainGOidnamespacecontents
A0004046molecular_functionaminoacylase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0016020cellular_componentmembrane
A0016324cellular_componentapical plasma membrane
A0016787molecular_functionhydrolase activity
A0016788molecular_functionhydrolase activity, acting on ester bonds
A0016811molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 319
ChainResidue
AHIS21
AGLU24
AHIS116
AACT324

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CS A 320
ChainResidue
AASN121
AASP248
AASP250

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CS A 321
ChainResidue
AGLY39
AGLN42

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CL A 322
ChainResidue
AALA120
AASN121
AGLN247
AASP248
AASP250
AILE282

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 323
ChainResidue
AHIS137
AHIS140

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE ACT A 324
ChainResidue
AHIS21
AGLU24
AARG63
AHIS116
AASN117
AGLU177
ATYR287
AZN319
AFMT325

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FMT A 325
ChainResidue
AHIS21
AARG63
AASN70
AARG71
ATYR287
AACT324

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues7
DetailsBINDING:
ChainResidueDetails
AHIS21
AGLU24
AASN70
AHIS116
AGLU177
ATYR287
AARG63

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q5M876
ChainResidueDetails
ATHR317

219869

PDB entries from 2024-05-15

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