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4PXC

The crystal structure of AtUAH in complex with (S)-hydroxyglycine

Functional Information from GO Data
ChainGOidnamespacecontents
A0000256biological_processallantoin catabolic process
A0004848molecular_functionureidoglycolate hydrolase activity
A0005783cellular_componentendoplasmic reticulum
A0006144biological_processpurine nucleobase metabolic process
A0006145biological_processpurine nucleobase catabolic process
A0009536cellular_componentplastid
A0010136biological_processureide catabolic process
A0016787molecular_functionhydrolase activity
A0016813molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
A0030145molecular_functionmanganese ion binding
A0046872molecular_functionmetal ion binding
A0047652molecular_functionallantoate deiminase activity
B0000256biological_processallantoin catabolic process
B0004848molecular_functionureidoglycolate hydrolase activity
B0005783cellular_componentendoplasmic reticulum
B0006144biological_processpurine nucleobase metabolic process
B0006145biological_processpurine nucleobase catabolic process
B0009536cellular_componentplastid
B0010136biological_processureide catabolic process
B0016787molecular_functionhydrolase activity
B0016813molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
B0030145molecular_functionmanganese ion binding
B0046872molecular_functionmetal ion binding
B0047652molecular_functionallantoate deiminase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 501
ChainResidue
AHIS138
AASP149
AHIS254
AHOH613
AHOH732
AHOH787

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 502
ChainResidue
AHGY503
AHOH689
AHOH732
AASP149
AGLU184
AHIS448

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE HGY A 503
ChainResidue
AGLU184
AARG353
AALA422
ATYR423
AHIS448
AMN502
AHOH689
AHOH732
BHIS290
BASN340

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MN B 501
ChainResidue
BHIS138
BASP149
BGLY150
BHIS254
BMN502
BHOH621
BHOH760
BHOH1080

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN B 502
ChainResidue
BASP149
BGLU184
BHIS448
BMN501
BHGY503
BHOH760

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE HGY B 503
ChainResidue
AHIS290
AASN340
BGLU184
BARG353
BALA422
BTYR423
BHIS448
BMN502
BHOH760
BHOH1080

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues230
DetailsRegion: {"description":"Involved in dimerization","evidences":[{"source":"PubMed","id":"25020232","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25020232","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4PXB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4PXC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4PXE","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25020232","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4PXB","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25020232","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4PXB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4PXC","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsSite: {"description":"Necessary for dimerization","evidences":[{"source":"UniProtKB","id":"Q53389","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

244693

PDB entries from 2025-11-12

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