Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1J70

CRYSTAL STRUCTURE OF YEAST ATP SULFURYLASE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000096	biological_process	sulfur amino acid metabolic process
A	0000103	biological_process	sulfate assimilation
A	0004781	molecular_function	sulfate adenylyltransferase (ATP) activity
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0006790	biological_process	sulfur compound metabolic process
A	0010134	biological_process	sulfate assimilation via adenylyl sulfate reduction
A	0016779	molecular_function	nucleotidyltransferase activity
A	0019379	biological_process	sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin)
A	0070814	biological_process	hydrogen sulfide biosynthetic process
B	0000096	biological_process	sulfur amino acid metabolic process
B	0000103	biological_process	sulfate assimilation
B	0004781	molecular_function	sulfate adenylyltransferase (ATP) activity
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0005739	cellular_component	mitochondrion
B	0006790	biological_process	sulfur compound metabolic process
B	0010134	biological_process	sulfate assimilation via adenylyl sulfate reduction
B	0016779	molecular_function	nucleotidyltransferase activity
B	0019379	biological_process	sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin)
B	0070814	biological_process	hydrogen sulfide biosynthetic process
C	0000096	biological_process	sulfur amino acid metabolic process
C	0000103	biological_process	sulfate assimilation
C	0004781	molecular_function	sulfate adenylyltransferase (ATP) activity
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0005739	cellular_component	mitochondrion
C	0006790	biological_process	sulfur compound metabolic process
C	0010134	biological_process	sulfate assimilation via adenylyl sulfate reduction
C	0016779	molecular_function	nucleotidyltransferase activity
C	0019379	biological_process	sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin)
C	0070814	biological_process	hydrogen sulfide biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PO4 C 2443

Chain	Residue
C	GLN195
C	THR196
C	ARG197
C	MET263
C	HIS274
C	HIS292
C	ALA293
C	HOH2516
C	HOH2687

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 B 2444

Chain	Residue
B	GLN195
B	THR196
B	ARG197
B	MET263
B	HIS292
B	ALA293
B	HOH2509

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PO4 A 2445

Chain	Residue
A	GLN195
A	THR196
A	ARG197
A	HIS274
A	HIS292
A	ALA293
A	HOH2472
A	HOH2560

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NA C 1759

Chain	Residue
C	THR38
C	PRO39
C	ARG40
C	TYR144

site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE NA C 1763

Chain	Residue
C	HIS433
C	ASN434

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE NA A 1765

Chain	Residue
A	PRO39
A	ARG40
A	TYR144

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	9
Details	ACT_SITE: ACT_SITE => ECO:0000255\|HAMAP-Rule:MF_03106, ECO:0000305\|PubMed:11157739

Chain	Residue	Details
A	THR196
A	ARG197
A	ASN198
B	THR196
B	ARG197
B	ASN198
C	THR196
C	ARG197
C	ASN198

site_id	SWS_FT_FI2
Number of Residues	15
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_03106, ECO:0000269\|PubMed:11157739

Chain	Residue	Details
A	GLN195
B	VAL331
C	GLN195
C	ARG197
C	GLY289
C	ALA293
C	VAL331
A	ARG197
A	GLY289
A	ALA293
A	VAL331
B	GLN195
B	ARG197
B	GLY289
B	ALA293

site_id	SWS_FT_FI3
Number of Residues	6
Details	SITE: Transition state stabilizer => ECO:0000255\|HAMAP-Rule:MF_03106, ECO:0000305\|PubMed:11157739

Chain	Residue	Details
A	HIS201
A	HIS204
B	HIS201
B	HIS204
C	HIS201
C	HIS204

site_id	SWS_FT_FI4
Number of Residues	3
Details	SITE: Induces change in substrate recognition on ATP binding => ECO:0000255\|HAMAP-Rule:MF_03106, ECO:0000305\|PubMed:11157739

Chain	Residue	Details
A	PHE328
B	PHE328
C	PHE328

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	a catalytic site defined by CSA, PubMed 11724564, 107174, 10506138, 11157739, 14983089, 9915785

Chain	Residue	Details
A	HIS204
A	HIS201
A	ARG197

site_id	CSA2
Number of Residues	3
Details	a catalytic site defined by CSA, PubMed 11724564, 107174, 10506138, 11157739, 14983089, 9915785

Chain	Residue	Details
B	HIS204
B	HIS201
B	ARG197

site_id	CSA3
Number of Residues	3
Details	a catalytic site defined by CSA, PubMed 11724564, 107174, 10506138, 11157739, 14983089, 9915785

Chain	Residue	Details
C	HIS204
C	HIS201
C	ARG197

site_id	MCSA1
Number of Residues	5
Details	M-CSA 287

Chain	Residue	Details
A	THR196	electrostatic stabiliser, hydrogen bond donor, steric role
A	ARG197	electrostatic stabiliser, hydrogen bond donor, steric role
A	HIS201	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	HIS204	electrostatic stabiliser
A	ARG290	electrostatic stabiliser

site_id	MCSA2
Number of Residues	5
Details	M-CSA 287

Chain	Residue	Details
B	THR196	electrostatic stabiliser, hydrogen bond donor, steric role
B	ARG197	electrostatic stabiliser, hydrogen bond donor, steric role
B	HIS201	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	HIS204	electrostatic stabiliser
B	ARG290	electrostatic stabiliser

site_id	MCSA3
Number of Residues	5
Details	M-CSA 287

Chain	Residue	Details
C	THR196	electrostatic stabiliser, hydrogen bond donor, steric role
C	ARG197	electrostatic stabiliser, hydrogen bond donor, steric role
C	HIS201	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
C	HIS204	electrostatic stabiliser
C	ARG290	electrostatic stabiliser

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)