Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1M54

CYSTATHIONINE-BETA SYNTHASE: REDUCED VICINAL THIOLS

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004122	molecular_function	cystathionine beta-synthase activity
A	0005737	cellular_component	cytoplasm
A	0006535	biological_process	cysteine biosynthetic process from serine
A	0019343	biological_process	cysteine biosynthetic process via cystathionine
B	0004122	molecular_function	cystathionine beta-synthase activity
B	0005737	cellular_component	cytoplasm
B	0006535	biological_process	cysteine biosynthetic process from serine
B	0019343	biological_process	cysteine biosynthetic process via cystathionine
C	0004122	molecular_function	cystathionine beta-synthase activity
C	0005737	cellular_component	cytoplasm
C	0006535	biological_process	cysteine biosynthetic process from serine
C	0019343	biological_process	cysteine biosynthetic process via cystathionine
D	0004122	molecular_function	cystathionine beta-synthase activity
D	0005737	cellular_component	cytoplasm
D	0006535	biological_process	cysteine biosynthetic process from serine
D	0019343	biological_process	cysteine biosynthetic process via cystathionine
E	0004122	molecular_function	cystathionine beta-synthase activity
E	0005737	cellular_component	cytoplasm
E	0006535	biological_process	cysteine biosynthetic process from serine
E	0019343	biological_process	cysteine biosynthetic process via cystathionine
F	0004122	molecular_function	cystathionine beta-synthase activity
F	0005737	cellular_component	cytoplasm
F	0006535	biological_process	cysteine biosynthetic process from serine
F	0019343	biological_process	cysteine biosynthetic process via cystathionine

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PLP A 1110

Chain	Residue
A	LYS119
A	GLY305
A	ILE306
A	SER349
A	PRO375
A	ASP376
A	ASN149
A	VAL255
A	GLY256
A	THR257
A	GLY258
A	GLY259
A	THR260
A	GLU304

site_id	AC2
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PLP B 1210

Chain	Residue
B	LYS119
B	ASN149
B	GLY256
B	THR257
B	GLY258
B	THR260
B	GLU304
B	GLY305
B	ILE306
B	SER349
B	PRO375
B	ASP376
B	TYR381

site_id	AC3
Number of Residues	15
Details	BINDING SITE FOR RESIDUE PLP C 1310

Chain	Residue
C	LYS119
C	ASN149
C	SER254
C	VAL255
C	GLY256
C	THR257
C	GLY258
C	GLY259
C	THR260
C	GLU304
C	GLY305
C	ILE306
C	SER349
C	PRO375
C	ASP376

site_id	AC4
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PLP D 1410

Chain	Residue
D	LYS119
D	ASN149
D	SER254
D	VAL255
D	GLY256
D	THR257
D	GLY258
D	GLY259
D	THR260
D	GLU304
D	GLY305
D	ILE306
D	SER349
D	PRO375

site_id	AC5
Number of Residues	16
Details	BINDING SITE FOR RESIDUE PLP E 1510

Chain	Residue
E	LYS119
E	ASN149
E	SER254
E	VAL255
E	GLY256
E	THR257
E	GLY258
E	GLY259
E	THR260
E	GLU304
E	GLY305
E	ILE306
E	SER349
E	PRO375
E	TYR381
E	HOH1523

site_id	AC6
Number of Residues	15
Details	BINDING SITE FOR RESIDUE PLP F 1610

Chain	Residue
F	LYS119
F	ASN149
F	SER254
F	VAL255
F	GLY256
F	THR257
F	GLY258
F	GLY259
F	THR260
F	GLY305
F	ILE306
F	SER349
F	PRO375
F	ASP376
F	TYR381

site_id	AC7
Number of Residues	16
Details	BINDING SITE FOR RESIDUE HEM A 1120

Chain	Residue
A	TYR233
A	ARG266
F	THR53
F	ARG58
A	ARG51
A	CYS52
A	THR53
A	TRP54
A	ARG58
A	GLU62
A	SER63
A	PRO64
A	HIS65
A	ALA226
A	PRO229
A	LEU230

site_id	AC8
Number of Residues	20
Details	BINDING SITE FOR RESIDUE HEM B 1220

Chain	Residue
B	PRO49
B	SER50
B	ARG51
B	CYS52
B	THR53
B	TRP54
B	ARG58
B	GLU62
B	SER63
B	PRO64
B	HIS65
B	ARG224
B	ALA226
B	PRO229
B	LEU230
B	TYR233
B	ARG266
D	THR53
D	ARG58
D	HEM1420

site_id	AC9
Number of Residues	14
Details	BINDING SITE FOR RESIDUE HEM C 1320

Chain	Residue
C	SER50
C	ARG51
C	CYS52
C	THR53
C	ARG58
C	GLU62
C	PRO64
C	HIS65
C	ALA226
C	PRO229
C	LEU230
C	TYR233
C	ARG266
E	ARG58

site_id	BC1
Number of Residues	17
Details	BINDING SITE FOR RESIDUE HEM D 1420

Chain	Residue
B	ARG58
B	HEM1220
D	PRO49
D	ARG51
D	CYS52
D	THR53
D	TRP54
D	ARG58
D	GLU62
D	SER63
D	PRO64
D	HIS65
D	ALA226
D	PRO229
D	LEU230
D	TYR233
D	ARG266

site_id	BC2
Number of Residues	16
Details	BINDING SITE FOR RESIDUE HEM E 1520

Chain	Residue
C	THR53
C	ARG58
E	SER50
E	ARG51
E	CYS52
E	TRP54
E	GLU62
E	SER63
E	PRO64
E	HIS65
E	ALA226
E	PRO229
E	LEU230
E	TYR233
E	ARG266
E	HOH1535

site_id	BC3
Number of Residues	16
Details	BINDING SITE FOR RESIDUE HEM F 1620

Chain	Residue
A	ARG58
F	ARG51
F	CYS52
F	THR53
F	TRP54
F	ARG58
F	GLU62
F	SER63
F	PRO64
F	HIS65
F	ARG224
F	ALA226
F	PRO229
F	LEU230
F	ARG266
F	VAL314

Functional Information from PROSITE/UniProt

site_id	PS00901
Number of Residues	19
Details	CYS_SYNTHASE Cysteine synthase/cystathionine beta-synthase P-phosphate attachment site. KcEffn.AGgSVKdRiSlrM

Chain	Residue	Details
A	LYS108-MET126

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"11483494","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12173932","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	36
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11483494","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12173932","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	6
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"11483494","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12173932","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	12
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)","evidences":[{"source":"PubMed","id":"17087506","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details

Chain	Residue	Details
A	LYS119

site_id	CSA2
Number of Residues	1
Details

Chain	Residue	Details
B	LYS119

site_id	CSA3
Number of Residues	1
Details

Chain	Residue	Details
C	LYS119

site_id	CSA4
Number of Residues	1
Details

Chain	Residue	Details
D	LYS119

site_id	CSA5
Number of Residues	1
Details

Chain	Residue	Details
E	LYS119

site_id	CSA6
Number of Residues	1
Details

Chain	Residue	Details
F	LYS119

site_id	MCSA1
Number of Residues	1
Details	M-CSA 713

Chain	Residue	Details
A	LYS119	covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay

site_id	MCSA2
Number of Residues	1
Details	M-CSA 713

Chain	Residue	Details
B	LYS119	covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay

site_id	MCSA3
Number of Residues	1
Details	M-CSA 713

Chain	Residue	Details
C	LYS119	covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay

site_id	MCSA4
Number of Residues	1
Details	M-CSA 713

Chain	Residue	Details
D	LYS119	covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay

site_id	MCSA5
Number of Residues	1
Details	M-CSA 713

Chain	Residue	Details
E	LYS119	covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay

site_id	MCSA6
Number of Residues	1
Details	M-CSA 713

Chain	Residue	Details
F	LYS119	covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay

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