4ZDP

The crystal structure of Y334C mutant of human SepSecS in complex with selenocysteine tRNA (tRNASec)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000049	molecular_function	tRNA binding
A	0001514	biological_process	selenocysteine incorporation
A	0001717	biological_process	conversion of seryl-tRNAsec to selenocys-tRNAsec
A	0003723	molecular_function	RNA binding
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006412	biological_process	translation
A	0016740	molecular_function	transferase activity
A	0098621	molecular_function	O-phosphoseryl-tRNA(Sec) selenium transferase activity
B	0000049	molecular_function	tRNA binding
B	0001514	biological_process	selenocysteine incorporation
B	0001717	biological_process	conversion of seryl-tRNAsec to selenocys-tRNAsec
B	0003723	molecular_function	RNA binding
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006412	biological_process	translation
B	0016740	molecular_function	transferase activity
B	0098621	molecular_function	O-phosphoseryl-tRNA(Sec) selenium transferase activity
C	0000049	molecular_function	tRNA binding
C	0001514	biological_process	selenocysteine incorporation
C	0001717	biological_process	conversion of seryl-tRNAsec to selenocys-tRNAsec
C	0003723	molecular_function	RNA binding
C	0005515	molecular_function	protein binding
C	0005634	cellular_component	nucleus
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006412	biological_process	translation
C	0016740	molecular_function	transferase activity
C	0098621	molecular_function	O-phosphoseryl-tRNA(Sec) selenium transferase activity
D	0000049	molecular_function	tRNA binding
D	0001514	biological_process	selenocysteine incorporation
D	0001717	biological_process	conversion of seryl-tRNAsec to selenocys-tRNAsec
D	0003723	molecular_function	RNA binding
D	0005515	molecular_function	protein binding
D	0005634	cellular_component	nucleus
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006412	biological_process	translation
D	0016740	molecular_function	transferase activity
D	0098621	molecular_function	O-phosphoseryl-tRNA(Sec) selenium transferase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	binding site for residue PLR A 1001

Chain	Residue
A	ARG75
A	ALA254
A	TYR255
A	LYS284
A	GLY312
A	ARG313
A	HOH1108
A	ALA143
A	THR144
A	GLY145
A	ILE170
A	GLN172
A	SER174
A	CYS175
A	ASN252

---

site_id	AC2
Number of Residues	3
Details	binding site for residue PO4 A 1002

Chain	Residue
A	ARG97
A	GLN105
A	HOH1163

---

site_id	AC3
Number of Residues	14
Details	binding site for residue PLR B 1001

Chain	Residue
B	ARG75
B	SER98
B	ALA143
B	THR144
B	GLY145
B	ILE170
B	GLN172
B	SER174
B	ASN252
B	TYR255
B	LYS284
B	GLY312
B	ARG313
B	HOH1175

---

site_id	AC4
Number of Residues	4
Details	binding site for residue PO4 B 1002

Chain	Residue
B	ARG97
B	GLN105
B	ARG313
B	HOH1136

---

site_id	AC5
Number of Residues	4
Details	binding site for residue PO4 C 1002

Chain	Residue
C	ARG97
C	GLN105
C	ARG313
C	HOH1148

---

site_id	AC6
Number of Residues	7
Details	binding site for residue PO4 D 1002

Chain	Residue
D	ARG97
D	SER98
D	GLN105
D	ARG313
D	HOH1105
D	HOH1108
D	HOH1125

---

site_id	AC7
Number of Residues	21
Details	binding site for Di-peptide PLR C 1001 and LYS C 284

Chain	Residue
C	ARG75
C	ALA143
C	THR144
C	GLY145
C	ILE170
C	GLN172
C	SER174
C	CYS175
C	ASN252
C	ALA254
C	TYR255
C	SER281
C	LEU282
C	ASP283
C	ASN285
C	GLY312
C	ARG313
C	HOH1102
C	HOH1103
C	HOH1117
C	HOH1127

---

site_id	AC8
Number of Residues	20
Details	binding site for Di-peptide PLR D 1001 and LYS D 284

Chain	Residue
D	GLU74
D	ARG75
D	SER98
D	ALA143
D	THR144
D	GLY145
D	GLN172
D	SER174
D	ASN252
D	ALA254
D	TYR255
D	SER281
D	LEU282
D	ASP283
D	ASN285
D	GLY312
D	ARG313
D	ILE440
D	HOH1103
D	HOH1120

---

Functional Information from PROSITE/UniProt

site_id	PS00435
Number of Residues	11
Details	PEROXIDASE_1 Peroxidases proximal heme-ligand signature. DIIKLAGVHTV

Chain	Residue	Details
A	ASP124-VAL134

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	40
Details	Region: {"description":"Phosphate loop (P-loop)","evidences":[{"source":"PubMed","id":"19608919","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	32
Details	Binding site: {"evidences":[{"source":"PubMed","id":"19608919","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Site: {"description":"May act as a substrate filter by repelling compounds with a negatively charged alpha-carboxylate","evidences":[{"source":"UniProtKB","id":"Q6P6M7","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"19608919","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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