6Y4Y

The crystal structure of human MACROD2 in space group P41212

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0015035	molecular_function	protein-disulfide reductase activity
A	0015036	molecular_function	disulfide oxidoreductase activity
A	0030337	molecular_function	DNA polymerase processivity factor activity
A	0045454	biological_process	cell redox homeostasis
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0015035	molecular_function	protein-disulfide reductase activity
B	0015036	molecular_function	disulfide oxidoreductase activity
B	0030337	molecular_function	DNA polymerase processivity factor activity
B	0045454	biological_process	cell redox homeostasis
C	0005515	molecular_function	protein binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0015035	molecular_function	protein-disulfide reductase activity
C	0015036	molecular_function	disulfide oxidoreductase activity
C	0030337	molecular_function	DNA polymerase processivity factor activity
C	0045454	biological_process	cell redox homeostasis
D	0005515	molecular_function	protein binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0015035	molecular_function	protein-disulfide reductase activity
D	0015036	molecular_function	disulfide oxidoreductase activity
D	0030337	molecular_function	DNA polymerase processivity factor activity
D	0045454	biological_process	cell redox homeostasis

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	binding site for residue TLA B 301

Chain	Residue
B	TRP11
B	ARG12
B	LYS15
B	HOH462
D	TRP11
D	ARG12
D	LYS15
D	HOH340

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Functional Information from PROSITE/UniProt

site_id	PS00194
Number of Residues	19
Details	THIOREDOXIN_1 Thioredoxin family active site. LVdFWaeWCGPCKmIapiL

Chain	Residue	Details
A	LEU-88-LEU-70

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	ACT_SITE: Nucleophile

Chain	Residue	Details
B	CYS-80
B	CYS-77
C	CYS-80
C	CYS-77
D	CYS-80
D	CYS-77
A	CYS-80
A	CYS-77

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site_id	SWS_FT_FI2
Number of Residues	4
Details	SITE: Deprotonates C-terminal active site Cys

Chain	Residue	Details
B	ASP-86
C	ASP-86
D	ASP-86
A	ASP-86

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site_id	SWS_FT_FI3
Number of Residues	8
Details	SITE: Contributes to redox potential value

Chain	Residue	Details
B	GLY-79
B	PRO-78
C	GLY-79
C	PRO-78
D	GLY-79
D	PRO-78
A	GLY-79
A	PRO-78

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842

Chain	Residue	Details
B	LYS-43
C	LYS-43
D	LYS-43
A	LYS-43

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site_id	SWS_FT_FI5
Number of Residues	20
Details	BINDING: BINDING => ECO:0000269|PubMed:23474712

Chain	Residue	Details
A	PHE224
B	GLY77
B	ALA90
B	GLY97
B	ILE185
B	PHE224
C	GLY77
C	ALA90
C	GLY97
C	ILE185
C	PHE224
D	GLY77
D	ALA90
D	GLY97
D	ILE185
D	PHE224
A	ALA90
A	GLY97
A	ILE185
A	GLY77

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site_id	SWS_FT_FI6
Number of Residues	8
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:18655026

Chain	Residue	Details
B	LYS170
C	LYS170
D	LYS170
A	LYS170

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