3U1K

Crystal structure of human PNPase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003676	molecular_function	nucleic acid binding
A	0003723	molecular_function	RNA binding
A	0004654	molecular_function	polyribonucleotide nucleotidyltransferase activity
A	0006396	biological_process	RNA processing
A	0006402	biological_process	mRNA catabolic process
B	0003676	molecular_function	nucleic acid binding
B	0003723	molecular_function	RNA binding
B	0004654	molecular_function	polyribonucleotide nucleotidyltransferase activity
B	0006396	biological_process	RNA processing
B	0006402	biological_process	mRNA catabolic process
C	0003676	molecular_function	nucleic acid binding
C	0003723	molecular_function	RNA binding
C	0004654	molecular_function	polyribonucleotide nucleotidyltransferase activity
C	0006396	biological_process	RNA processing
C	0006402	biological_process	mRNA catabolic process
D	0003676	molecular_function	nucleic acid binding
D	0003723	molecular_function	RNA binding
D	0004654	molecular_function	polyribonucleotide nucleotidyltransferase activity
D	0006396	biological_process	RNA processing
D	0006402	biological_process	mRNA catabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE CIT A 1

Chain	Residue
A	HOH9
A	HOH673
A	PHE429
A	HIS450
A	GLY481
A	SER482
A	SER483
A	SER484
A	ASP544
A	LYS546

---

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE CIT A 670

Chain	Residue
A	ARG132
A	ARG446
A	HIS450
A	ASP538
A	ASP544
A	LYS546
A	ASP560
A	HOH802

---

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE CIT C 1

Chain	Residue
C	ARG132
C	ARG446
C	HIS450
C	ASP538
C	ASP544
C	LYS546
C	ASP560
C	HOH982

---

site_id	AC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE CIT C 670

Chain	Residue
C	HOH24
C	PHE429
C	ARG446
C	HIS450
C	GLY481
C	SER482
C	SER483
C	SER484
C	ASP544
C	LYS546
C	HOH732
C	HOH850

---

site_id	AC5
Number of Residues	12
Details	BINDING SITE FOR RESIDUE CIT B 1

Chain	Residue
B	HOH12
B	PHE429
B	HIS450
B	GLY481
B	SER482
B	SER483
B	SER484
B	ASP544
B	LYS546
B	HOH717
B	HOH804
B	HOH908

---

site_id	AC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE CIT B 670

Chain	Residue
B	ARG132
B	ARG446
B	HIS450
B	ASP538
B	ASP544
B	LYS546
B	ASP560
B	HOH747
B	HOH908

---

site_id	AC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE CIT D 1

Chain	Residue
D	ARG132
D	ARG446
D	HIS450
D	ASP538
D	ASP544
D	LYS546
D	ASP560
D	CIT670

---

site_id	AC8
Number of Residues	13
Details	BINDING SITE FOR RESIDUE CIT D 670

Chain	Residue
D	CIT1
D	PHE429
D	ARG446
D	HIS450
D	GLY481
D	SER482
D	SER483
D	SER484
D	ASP544
D	LYS546
D	HOH683
D	HOH735
D	HOH871

---

Functional Information from PROSITE/UniProt

site_id	PS00659
Number of Residues	10
Details	GLYCOSYL_HYDROL_F5 Glycosyl hydrolases family 5 signature. LAVDGVNEPD

Chain	Residue	Details
A	LEU157-ASP166

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q8K1R3

Chain	Residue	Details
A	LYS250
C	LYS250
B	LYS250
D	LYS250

---

site_id	SWS_FT_FI2
Number of Residues	12
Details	MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861

Chain	Residue	Details
A	LYS264
D	LYS264
D	LYS285
D	LYS289
A	LYS285
A	LYS289
C	LYS264
C	LYS285
C	LYS289
B	LYS264
B	LYS285
B	LYS289

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q8K1R3

Chain	Residue	Details
A	LYS552
C	LYS552
B	LYS552
D	LYS552

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