Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6LUR

Human PUF60 UHM domain (thioredoxin fusion) in complex with a small molecule binder

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003676	molecular_function	nucleic acid binding
A	0003723	molecular_function	RNA binding
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	0003676	molecular_function	nucleic acid binding
B	0003723	molecular_function	RNA binding
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	0003676	molecular_function	nucleic acid binding
C	0003723	molecular_function	RNA binding
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	0003676	molecular_function	nucleic acid binding
D	0003723	molecular_function	RNA binding
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
E	0003676	molecular_function	nucleic acid binding
E	0003723	molecular_function	RNA binding
E	0005515	molecular_function	protein binding
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0015035	molecular_function	protein-disulfide reductase activity
E	0015036	molecular_function	disulfide oxidoreductase activity
E	0030337	molecular_function	DNA polymerase processivity factor activity
E	0045454	biological_process	cell redox homeostasis
F	0003676	molecular_function	nucleic acid binding
F	0003723	molecular_function	RNA binding
F	0005515	molecular_function	protein binding
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0015035	molecular_function	protein-disulfide reductase activity
F	0015036	molecular_function	disulfide oxidoreductase activity
F	0030337	molecular_function	DNA polymerase processivity factor activity
F	0045454	biological_process	cell redox homeostasis
G	0003676	molecular_function	nucleic acid binding
G	0003723	molecular_function	RNA binding
G	0005515	molecular_function	protein binding
G	0005737	cellular_component	cytoplasm
G	0005829	cellular_component	cytosol
G	0015035	molecular_function	protein-disulfide reductase activity
G	0015036	molecular_function	disulfide oxidoreductase activity
G	0030337	molecular_function	DNA polymerase processivity factor activity
G	0045454	biological_process	cell redox homeostasis
H	0003676	molecular_function	nucleic acid binding
H	0003723	molecular_function	RNA binding
H	0005515	molecular_function	protein binding
H	0005737	cellular_component	cytoplasm
H	0005829	cellular_component	cytosol
H	0015035	molecular_function	protein-disulfide reductase activity
H	0015036	molecular_function	disulfide oxidoreductase activity
H	0030337	molecular_function	DNA polymerase processivity factor activity
H	0045454	biological_process	cell redox homeostasis

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	binding site for residue EVU B 601

Chain	Residue
B	MET466
B	LEU476
B	GLU479
B	VAL480
B	GLU483
B	PHE534
B	HOH773

site_id	AC2
Number of Residues	6
Details	binding site for residue EVU B 602

Chain	Residue
B	ILE508
C	LEU361
C	LYS362
C	GLY428
B	LYS499
B	GLU504

site_id	AC3
Number of Residues	5
Details	binding site for residue EVU B 603

Chain	Residue
B	ALA449
B	GLY453
B	SER454
B	ALA455
F	MET381

site_id	AC4
Number of Residues	6
Details	binding site for residue EVU C 601

Chain	Residue
C	MET466
C	LEU476
C	GLU479
C	GLU483
C	CYS484
C	PHE534

site_id	AC5
Number of Residues	4
Details	binding site for residue EVU C 602

Chain	Residue
C	ALA449
C	GLY453
C	SER454
C	ALA455

site_id	AC6
Number of Residues	5
Details	binding site for residue EVU D 601

Chain	Residue
D	MET466
D	GLU479
D	GLU483
D	CYS484
D	PHE534

site_id	AC7
Number of Residues	6
Details	binding site for residue EVU D 602

Chain	Residue
A	LYS499
A	ILE508
D	ASP357
D	LEU361
D	LYS362
D	GLY428

site_id	AC8
Number of Residues	7
Details	binding site for residue EVU E 601

Chain	Residue
E	LEU463
E	MET466
E	LEU476
E	GLU479
E	VAL480
E	GLU483
E	PHE534

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU368-LEU386

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	16
Details	ACT_SITE: Nucleophile

Chain	Residue	Details
A	CYS376
E	CYS379
F	CYS376
F	CYS379
G	CYS376
G	CYS379
H	CYS376
H	CYS379
A	CYS379
B	CYS376
B	CYS379
C	CYS376
C	CYS379
D	CYS376
D	CYS379
E	CYS376

site_id	SWS_FT_FI2
Number of Residues	8
Details	SITE: Deprotonates C-terminal active site Cys

Chain	Residue	Details
A	ASP370
B	ASP370
C	ASP370
D	ASP370
E	ASP370
F	ASP370
G	ASP370
H	ASP370

site_id	SWS_FT_FI3
Number of Residues	16
Details	SITE: Contributes to redox potential value

Chain	Residue	Details
A	GLY377
E	PRO378
F	GLY377
F	PRO378
G	GLY377
G	PRO378
H	GLY377
H	PRO378
A	PRO378
B	GLY377
B	PRO378
C	GLY377
C	PRO378
D	GLY377
D	PRO378
E	GLY377

site_id	SWS_FT_FI4
Number of Residues	8
Details	MOD_RES: N6-acetyllysine => ECO:0000269\|PubMed:18723842

Chain	Residue	Details
A	LYS413
B	LYS413
C	LYS413
D	LYS413
E	LYS413
F	LYS413
G	LYS413
H	LYS413

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)