Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2Z67

Crystal structure of archaeal O-phosphoseryl-tRNA(Sec) selenium transferase (SepSecS)

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	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	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	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	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	5
Details	BINDING SITE FOR RESIDUE SO4 B 1002

Chain	Residue
B	ARG94
B	SER95
B	GLN102
B	ARG307
B	HOH1005

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 C 1002

Chain	Residue
C	ARG94
C	SER95
C	GLN102
C	ARG307

site_id	AC3
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PLP A 1001

Chain	Residue
A	SER138
A	THR139
A	GLY140
A	HIS166
A	SER168
A	THR220
A	ASN247
A	ALA249
A	TYR250
A	LYS278
B	GLU71
B	ARG72
B	GLY306
B	ARG307

site_id	AC4
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PLP B 1001

Chain	Residue
A	ARG72
A	GLY306
A	ARG307
B	SER138
B	THR139
B	GLY140
B	HIS166
B	SER168
B	THR220
B	PHE221
B	ASN247
B	ALA249
B	LYS278
B	HOH1029

site_id	AC5
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PLP C 1001

Chain	Residue
C	SER138
C	THR139
C	GLY140
C	HIS166
C	SER168
C	THR220
C	PHE221
C	ASN247
C	TYR250
C	LYS278
D	ARG72
D	GLY306
D	ARG307

site_id	AC6
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PLP D 1001

Chain	Residue
C	ARG72
C	GLY306
C	ARG307
D	SER138
D	THR139
D	GLY140
D	HIS166
D	SER168
D	THR220
D	PHE221
D	ASN247
D	ALA249
D	LYS278

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	40
Details	Region: {"description":"Phosphate loop (P-loop)","evidences":[{"source":"UniProtKB","id":"Q6P6M7","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	20
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18158303","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":[{"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":"17142313","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18158303","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1qgn

Chain	Residue	Details
A	LYS278
A	ASN247
A	TYR163

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1qgn

Chain	Residue	Details
B	LYS278
B	ASN247
B	TYR163

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1qgn

Chain	Residue	Details
C	LYS278
C	ASN247
C	TYR163

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1qgn

Chain	Residue	Details
D	LYS278
D	ASN247
D	TYR163

site_id	MCSA1
Number of Residues	8
Details	M-CSA 286

Chain	Residue	Details
A	PHE88	attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor
A	ILE110	attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor
A	MSE111	electrostatic stabiliser, hydrogen bond donor
A	ILE118	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
A	ASP190	electrostatic stabiliser, polar interaction
A	LEU281	steric role, van der waals interaction
A	ALA310	activator, covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, polar interaction, proton acceptor, proton donor
A	LYS339	attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor

site_id	MCSA2
Number of Residues	8
Details	M-CSA 286

Chain	Residue	Details
B	PHE88	attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor
B	ILE110	attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor
B	MSE111	electrostatic stabiliser, hydrogen bond donor
B	ILE118	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
B	ASP190	electrostatic stabiliser, polar interaction
B	LEU281	steric role, van der waals interaction
B	ALA310	activator, covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, polar interaction, proton acceptor, proton donor
B	LYS339	attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor

site_id	MCSA3
Number of Residues	8
Details	M-CSA 286

Chain	Residue	Details
C	PHE88	attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor
C	ILE110	attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor
C	MSE111	electrostatic stabiliser, hydrogen bond donor
C	ILE118	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
C	ASP190	electrostatic stabiliser, polar interaction
C	LEU281	steric role, van der waals interaction
C	ALA310	activator, covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, polar interaction, proton acceptor, proton donor
C	LYS339	attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor

site_id	MCSA4
Number of Residues	8
Details	M-CSA 286

Chain	Residue	Details
D	PHE88	attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor
D	ILE110	attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor
D	MSE111	electrostatic stabiliser, hydrogen bond donor
D	ILE118	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
D	ASP190	electrostatic stabiliser, polar interaction
D	LEU281	steric role, van der waals interaction
D	ALA310	activator, covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, polar interaction, proton acceptor, proton donor
D	LYS339	attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor

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