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6AZN

Structural and biochemical characterization of a non-canonical biuret hydrolase (BiuH) from the cyanuric acid catabolism pathway of Rhizobium leguminasorum bv. viciae 3841

Functional Information from GO Data
ChainGOidnamespacecontents
A0016787molecular_functionhydrolase activity
B0016787molecular_functionhydrolase activity
C0016787molecular_functionhydrolase activity
D0016787molecular_functionhydrolase activity
F0016787molecular_functionhydrolase activity
G0016787molecular_functionhydrolase activity
H0016787molecular_functionhydrolase activity
I0016787molecular_functionhydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue EDO A 301
ChainResidue
AARG186
AGLY187
ATYR188
AHOH451
AHOH505

site_idAC2
Number of Residues6
Detailsbinding site for residue PO4 A 302
ChainResidue
BARG186
BTYR188
AASN158
AGLN159
AARG161
BASN158

site_idAC3
Number of Residues5
Detailsbinding site for residue EDO C 301
ChainResidue
CASN158
CGLN159
CARG161
DARG186
DTYR188

site_idAC4
Number of Residues6
Detailsbinding site for residue PO4 F 301
ChainResidue
FARG186
FGLY187
FTYR188
GASN158
GGLN159
GARG161

site_idAC5
Number of Residues3
Detailsbinding site for residue EDO I 301
ChainResidue
ICYS42
IGLU130
IHOH521

site_idAC6
Number of Residues4
Detailsbinding site for residue EDO I 302
ChainResidue
HARG186
HTYR188
IGLN159
IARG161

site_idAC7
Number of Residues6
Detailsbinding site for residue PO4 I 303
ChainResidue
HASN158
HGLN159
HARG161
IARG186
IGLY187
ITYR188

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:29425231
ChainResidueDetails
AASP36
BASP36
CASP36
DASP36
FASP36
GASP36
HASP36
IASP36

site_idSWS_FT_FI2
Number of Residues8
DetailsACT_SITE: ACT_SITE => ECO:0000305|PubMed:29425231
ChainResidueDetails
ALYS142
BLYS142
CLYS142
DLYS142
FLYS142
GLYS142
HLYS142
ILYS142

site_idSWS_FT_FI3
Number of Residues8
DetailsACT_SITE: Nucleophile => ECO:0000305|PubMed:29425231
ChainResidueDetails
ASER175
BSER175
CSER175
DSER175
FSER175
GSER175
HSER175
ISER175

site_idSWS_FT_FI4
Number of Residues32
DetailsBINDING: BINDING => ECO:0000269|PubMed:29425231, ECO:0007744|PDB:6AZQ
ChainResidueDetails
AGLU84
CLYS145
CILE170
CGLN215
DGLU84
DLYS145
DILE170
DGLN215
FGLU84
FLYS145
FILE170
ALYS145
FGLN215
GGLU84
GLYS145
GILE170
GGLN215
HGLU84
HLYS145
HILE170
HGLN215
IGLU84
AILE170
ILYS145
IILE170
IGLN215
AGLN215
BGLU84
BLYS145
BILE170
BGLN215
CGLU84

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PDB entries from 2024-10-02

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