Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

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
DetailsACT_SITE:
ChainResidueDetails
AGLU174
EHIS248
FGLU174
FHIS248
AHIS248
BGLU174
BHIS248
CGLU174
CHIS248
DGLU174
DHIS248
EGLU174

site_idSWS_FT_FI2
Number of Residues6
DetailsACT_SITE: Nucleophile
ChainResidueDetails
ACYS365
BCYS365
CCYS365
DCYS365
ECYS365
FCYS365

site_idSWS_FT_FI3
Number of Residues36
DetailsBINDING:
ChainResidueDetails
AALA19
BARG212
BASP250
BASN359
CALA19
CASN110
CHIS137
CARG212
CASP250
CASN359
DALA19
AASN110
DASN110
DHIS137
DARG212
DASP250
DASN359
EALA19
EASN110
EHIS137
EARG212
EASP250
AHIS137
EASN359
FALA19
FASN110
FHIS137
FARG212
FASP250
FASN359
AARG212
AASP250
AASN359
BALA19
BASN110
BHIS137

237735

PDB entries from 2025-06-18

PDB statisticsPDBj update infoContact PDBjnumon