5AYR

The crystal structure of SAUGI/human UDG complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004844	molecular_function	uracil DNA N-glycosylase activity
A	0006281	biological_process	DNA repair
A	0006284	biological_process	base-excision repair
A	0016799	molecular_function	hydrolase activity, hydrolyzing N-glycosyl compounds
B	0046872	molecular_function	metal ion binding
C	0004844	molecular_function	uracil DNA N-glycosylase activity
C	0006281	biological_process	DNA repair
C	0006284	biological_process	base-excision repair
C	0016799	molecular_function	hydrolase activity, hydrolyzing N-glycosyl compounds
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue MG A 900

Chain	Residue
A	ASP145
A	ASN215
A	HOH1006
A	HOH1009
A	HOH1071
B	HOH1008

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site_id	AC2
Number of Residues	6
Details	binding site for residue MG B 900

Chain	Residue
B	HOH1027
D	ASP88
D	MG900
B	ASP88
B	MET89
B	HOH1015

---

site_id	AC3
Number of Residues	6
Details	binding site for residue MG C 900

Chain	Residue
C	ASP145
C	ASN215
C	HOH1007
C	HOH1009
C	HOH1029
C	HOH1071

---

site_id	AC4
Number of Residues	6
Details	binding site for residue MG D 900

Chain	Residue
B	ASP88
B	MG900
B	HOH1015
D	ASP88
D	MET89
D	HOH1007

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Functional Information from PROSITE/UniProt

site_id	PS00130
Number of Residues	10
Details	U_DNA_GLYCOSYLASE Uracil-DNA glycosylase signature. KVVIlGQDPY

Chain	Residue	Details
A	LYS138-TYR147

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_03166, ECO:0000269|PubMed:9724657, ECO:0000312|PDB:1SSP

Chain	Residue	Details
A	ASP145
C	ASP145

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site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|PubMed:8900285, ECO:0000269|PubMed:9724657, ECO:0000312|PDB:1SSP, ECO:0000312|PDB:4SKN

Chain	Residue	Details
A	GLN144
A	PHE158
A	ASN204
A	HIS268
C	GLN144
C	PHE158
C	ASN204
C	HIS268

---

site_id	SWS_FT_FI3
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269|PubMed:8900285, ECO:0000312|PDB:4SKN

Chain	Residue	Details
A	HIS148
C	SER270
C	SER273
C	ARG276
A	SER169
A	SER247
A	SER270
A	SER273
A	ARG276
C	HIS148
C	SER169
C	SER247

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861

Chain	Residue	Details
A	LYS286
C	LYS286

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