Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5CB6

Structure of adenosine-5'-phosphosulfate kinase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000103	biological_process	sulfate assimilation
A	0000166	molecular_function	nucleotide binding
A	0004020	molecular_function	adenylylsulfate kinase activity
A	0004781	molecular_function	sulfate adenylyltransferase (ATP) activity
A	0005524	molecular_function	ATP binding
A	0016301	molecular_function	kinase activity
A	0016740	molecular_function	transferase activity
A	0019379	biological_process	sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin)
A	0070814	biological_process	hydrogen sulfide biosynthetic process
B	0000103	biological_process	sulfate assimilation
B	0000166	molecular_function	nucleotide binding
B	0004020	molecular_function	adenylylsulfate kinase activity
B	0004781	molecular_function	sulfate adenylyltransferase (ATP) activity
B	0005524	molecular_function	ATP binding
B	0016301	molecular_function	kinase activity
B	0016740	molecular_function	transferase activity
B	0019379	biological_process	sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin)
B	0070814	biological_process	hydrogen sulfide biosynthetic process
C	0000103	biological_process	sulfate assimilation
C	0000166	molecular_function	nucleotide binding
C	0004020	molecular_function	adenylylsulfate kinase activity
C	0004781	molecular_function	sulfate adenylyltransferase (ATP) activity
C	0005524	molecular_function	ATP binding
C	0016301	molecular_function	kinase activity
C	0016740	molecular_function	transferase activity
C	0019379	biological_process	sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin)
C	0070814	biological_process	hydrogen sulfide biosynthetic process
D	0000103	biological_process	sulfate assimilation
D	0000166	molecular_function	nucleotide binding
D	0004020	molecular_function	adenylylsulfate kinase activity
D	0004781	molecular_function	sulfate adenylyltransferase (ATP) activity
D	0005524	molecular_function	ATP binding
D	0016301	molecular_function	kinase activity
D	0016740	molecular_function	transferase activity
D	0019379	biological_process	sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin)
D	0070814	biological_process	hydrogen sulfide biosynthetic process
E	0000103	biological_process	sulfate assimilation
E	0000166	molecular_function	nucleotide binding
E	0004020	molecular_function	adenylylsulfate kinase activity
E	0004781	molecular_function	sulfate adenylyltransferase (ATP) activity
E	0005524	molecular_function	ATP binding
E	0016301	molecular_function	kinase activity
E	0016740	molecular_function	transferase activity
E	0019379	biological_process	sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin)
E	0070814	biological_process	hydrogen sulfide biosynthetic process
F	0000103	biological_process	sulfate assimilation
F	0000166	molecular_function	nucleotide binding
F	0004020	molecular_function	adenylylsulfate kinase activity
F	0004781	molecular_function	sulfate adenylyltransferase (ATP) activity
F	0005524	molecular_function	ATP binding
F	0016301	molecular_function	kinase activity
F	0016740	molecular_function	transferase activity
F	0019379	biological_process	sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin)
F	0070814	biological_process	hydrogen sulfide biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	binding site for residue ADX A 301

Chain	Residue
A	GLY41
A	SER86
A	PRO87
A	LEU122
A	GLY133
A	PHE134
A	THR135
A	ANP302
A	HOH419
A	ASP42
A	ARG45
A	PHE54
A	ARG59
A	ASN62
A	ILE63
A	ALA84
A	ILE85

site_id	AC2
Number of Residues	20
Details	binding site for residue ANP A 302

Chain	Residue
A	LEU13
A	SER14
A	GLY15
A	ALA16
A	GLY17
A	LYS18
A	THR19
A	THR20
A	ASP42
A	ARG117
A	LYS120
A	THR153
A	GLU156
A	SER161
A	ADX301
A	MG303
A	NA304
A	HOH402
A	HOH414
A	HOH419

site_id	AC3
Number of Residues	5
Details	binding site for residue MG A 303

Chain	Residue
A	THR19
A	ASP40
A	ASP42
A	ANP302
A	HOH402

site_id	AC4
Number of Residues	8
Details	binding site for residue NA A 304

Chain	Residue
A	THR153
A	ASP154
A	GLU156
A	ANP302
B	THR153
B	ASP154
B	GLU156
B	ANP302

site_id	AC5
Number of Residues	17
Details	binding site for residue ADX B 301

Chain	Residue
B	GLY41
B	ASP42
B	ARG45
B	PHE54
B	ARG59
B	ASN62
B	ILE63
B	ALA84
B	ILE85
B	SER86
B	PRO87
B	LEU122
B	GLY133
B	PHE134
B	THR135
B	ANP302
B	HOH401

site_id	AC6
Number of Residues	20
Details	binding site for residue ANP B 302

Chain	Residue
A	GLU156
A	GLU157
A	NA304
B	GLY15
B	GLY17
B	LYS18
B	THR19
B	THR20
B	ASP42
B	ARG117
B	LYS120
B	THR153
B	GLU156
B	GLU157
B	LEU158
B	SER161
B	ADX301
B	MG303
B	HOH401
B	HOH402

site_id	AC7
Number of Residues	4
Details	binding site for residue MG B 303

Chain	Residue
B	THR19
B	LYS120
B	ANP302
B	HOH402

site_id	AC8
Number of Residues	18
Details	binding site for residue ADX C 301

Chain	Residue
C	SER86
C	PRO87
C	LYS120
C	LEU122
C	LYS132
C	GLY133
C	PHE134
C	THR135
C	ANP302
C	HOH401
C	SER14
C	ASP42
C	ARG45
C	PHE54
C	ARG59
C	ASN62
C	ALA84
C	ILE85

site_id	AC9
Number of Residues	18
Details	binding site for residue ANP C 302

Chain	Residue
C	LEU13
C	GLY15
C	ALA16
C	GLY17
C	LYS18
C	THR19
C	THR20
C	ASP42
C	ARG117
C	VAL119
C	LYS120
C	THR153
C	GLU156
C	SER161
C	ADX301
C	MG303
C	HOH401
C	HOH404

site_id	AD1
Number of Residues	4
Details	binding site for residue MG C 303

Chain	Residue
C	THR19
C	ASP40
C	ASP42
C	ANP302

site_id	AD2
Number of Residues	3
Details	binding site for residue CAC C 304

Chain	Residue
B	ASP138
C	ASP138
F	ASP138

site_id	AD3
Number of Residues	17
Details	binding site for residue ADX D 301

Chain	Residue
D	GLY41
D	ASP42
D	ARG45
D	PHE54
D	ARG59
D	ASN62
D	ILE63
D	ALA84
D	ILE85
D	SER86
D	PRO87
D	LEU122
D	GLY133
D	PHE134
D	THR135
D	ANP302
D	HOH402

site_id	AD4
Number of Residues	18
Details	binding site for residue ANP D 302

Chain	Residue
D	LEU13
D	SER14
D	GLY15
D	ALA16
D	GLY17
D	LYS18
D	THR19
D	THR20
D	ASP42
D	ARG117
D	VAL119
D	THR153
D	GLU156
D	ADX301
D	MG303
D	HOH402
D	HOH406
D	HOH408

site_id	AD5
Number of Residues	4
Details	binding site for residue MG D 303

Chain	Residue
D	THR19
D	ASP40
D	ASP42
D	ANP302

site_id	AD6
Number of Residues	3
Details	binding site for residue CAC D 304

Chain	Residue
A	ASP138
D	ASP138
E	ASP138

site_id	AD7
Number of Residues	18
Details	binding site for residue ADX E 301

Chain	Residue
E	SER14
E	ASP42
E	ARG45
E	PHE54
E	ARG59
E	ASN62
E	ILE63
E	ALA84
E	ILE85
E	SER86
E	PRO87
E	LYS120
E	LEU122
E	LYS132
E	GLY133
E	PHE134
E	THR135
E	ANP302

site_id	AD8
Number of Residues	17
Details	binding site for residue ANP E 302

Chain	Residue
E	LEU13
E	SER14
E	GLY15
E	ALA16
E	GLY17
E	LYS18
E	THR19
E	THR20
E	ASP42
E	ARG117
E	LYS120
E	THR153
E	GLU156
E	SER161
E	ADX301
E	MG303
E	HOH402

site_id	AD9
Number of Residues	5
Details	binding site for residue MG E 303

Chain	Residue
E	THR19
E	ASP40
E	ASP42
E	ANP302
E	HOH402

site_id	AE1
Number of Residues	17
Details	binding site for residue ADX F 301

Chain	Residue
F	GLY41
F	ASP42
F	ARG45
F	PHE54
F	ARG59
F	ASN62
F	ILE63
F	ALA84
F	ILE85
F	SER86
F	PRO87
F	LYS120
F	LEU122
F	GLY133
F	PHE134
F	THR135
F	ANP302

site_id	AE2
Number of Residues	21
Details	binding site for residue ANP F 302

Chain	Residue
F	LEU13
F	SER14
F	GLY15
F	ALA16
F	GLY17
F	LYS18
F	THR19
F	THR20
F	ASP42
F	ILE85
F	ARG117
F	LYS120
F	THR153
F	GLU156
F	GLU157
F	LEU158
F	SER161
F	ADX301
F	MG303
F	HOH402
F	HOH406

site_id	AE3
Number of Residues	5
Details	binding site for residue MG F 303

Chain	Residue
F	THR19
F	ASP40
F	ASP42
F	ANP302
F	HOH406

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Active site: {"description":"Phosphoserine intermediate","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	42
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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