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1YNF

Crystal Structure of N-Succinylarginine Dihydrolase, AstB, bound to Substrate and Product, an Enzyme from the Arginine Catabolic Pathway of Escherichia coli

Functional Information from GO Data
ChainGOidnamespacecontents
A0006525biological_processarginine metabolic process
A0006527biological_processL-arginine catabolic process
A0009015molecular_functionN-succinylarginine dihydrolase activity
A0016787molecular_functionhydrolase activity
A0019544biological_processL-arginine catabolic process to L-glutamate
A0019545biological_processL-arginine catabolic process to succinate
A0042803molecular_functionprotein homodimerization activity
B0006525biological_processarginine metabolic process
B0006527biological_processL-arginine catabolic process
B0009015molecular_functionN-succinylarginine dihydrolase activity
B0016787molecular_functionhydrolase activity
B0019544biological_processL-arginine catabolic process to L-glutamate
B0019545biological_processL-arginine catabolic process to succinate
B0042803molecular_functionprotein homodimerization activity
C0006525biological_processarginine metabolic process
C0006527biological_processL-arginine catabolic process
C0009015molecular_functionN-succinylarginine dihydrolase activity
C0016787molecular_functionhydrolase activity
C0019544biological_processL-arginine catabolic process to L-glutamate
C0019545biological_processL-arginine catabolic process to succinate
C0042803molecular_functionprotein homodimerization activity
D0006525biological_processarginine metabolic process
D0006527biological_processL-arginine catabolic process
D0009015molecular_functionN-succinylarginine dihydrolase activity
D0016787molecular_functionhydrolase activity
D0019544biological_processL-arginine catabolic process to L-glutamate
D0019545biological_processL-arginine catabolic process to succinate
D0042803molecular_functionprotein homodimerization activity
E0006525biological_processarginine metabolic process
E0006527biological_processL-arginine catabolic process
E0009015molecular_functionN-succinylarginine dihydrolase activity
E0016787molecular_functionhydrolase activity
E0019544biological_processL-arginine catabolic process to L-glutamate
E0019545biological_processL-arginine catabolic process to succinate
E0042803molecular_functionprotein homodimerization activity
F0006525biological_processarginine metabolic process
F0006527biological_processL-arginine catabolic process
F0009015molecular_functionN-succinylarginine dihydrolase activity
F0016787molecular_functionhydrolase activity
F0019544biological_processL-arginine catabolic process to L-glutamate
F0019545biological_processL-arginine catabolic process to succinate
F0042803molecular_functionprotein homodimerization activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K E 448
ChainResidue
ELEU338
ELEU339
EALA341
EASN343
EILE345

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K C 448
ChainResidue
CILE345
CLEU338
CLEU339
CALA341
CASN343

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K B 448
ChainResidue
BLEU338
BLEU339
BALA341
BASN343
BILE345
BHOH620

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K A 448
ChainResidue
ALEU338
ALEU339
AALA341
AASN343
AILE345
AHOH620

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K F 448
ChainResidue
FLEU338
FLEU339
FALA341
FASN343
FILE345

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K D 448
ChainResidue
DLEU338
DLEU339
DALA341
DASN343
DILE345

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsActive site: {}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsActive site: {"description":"Nucleophile"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues30
DetailsBinding site: {}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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