Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6I35

Crystal structure of human glycine decarboxylase (P-protein) bound with pyridoxyl-glycine-5'-monophosphate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004375	molecular_function	glycine dehydrogenase (decarboxylating) activity
A	0005739	cellular_component	mitochondrion
A	0005759	cellular_component	mitochondrial matrix
A	0005960	cellular_component	glycine cleavage complex
A	0006520	biological_process	amino acid metabolic process
A	0006544	biological_process	glycine metabolic process
A	0006546	biological_process	glycine catabolic process
A	0009055	molecular_function	electron transfer activity
A	0016491	molecular_function	oxidoreductase activity
A	0016594	molecular_function	glycine binding
A	0016829	molecular_function	lyase activity
A	0019464	biological_process	glycine decarboxylation via glycine cleavage system
A	0030170	molecular_function	pyridoxal phosphate binding
A	0036255	biological_process	response to methylamine
A	0042803	molecular_function	protein homodimerization activity
A	0070280	molecular_function	pyridoxal binding
A	1903442	biological_process	response to lipoic acid
B	0004375	molecular_function	glycine dehydrogenase (decarboxylating) activity
B	0005739	cellular_component	mitochondrion
B	0005759	cellular_component	mitochondrial matrix
B	0005960	cellular_component	glycine cleavage complex
B	0006520	biological_process	amino acid metabolic process
B	0006544	biological_process	glycine metabolic process
B	0006546	biological_process	glycine catabolic process
B	0009055	molecular_function	electron transfer activity
B	0016491	molecular_function	oxidoreductase activity
B	0016594	molecular_function	glycine binding
B	0016829	molecular_function	lyase activity
B	0019464	biological_process	glycine decarboxylation via glycine cleavage system
B	0030170	molecular_function	pyridoxal phosphate binding
B	0036255	biological_process	response to methylamine
B	0042803	molecular_function	protein homodimerization activity
B	0070280	molecular_function	pyridoxal binding
B	1903442	biological_process	response to lipoic acid
C	0004375	molecular_function	glycine dehydrogenase (decarboxylating) activity
C	0005739	cellular_component	mitochondrion
C	0005759	cellular_component	mitochondrial matrix
C	0005960	cellular_component	glycine cleavage complex
C	0006520	biological_process	amino acid metabolic process
C	0006544	biological_process	glycine metabolic process
C	0006546	biological_process	glycine catabolic process
C	0009055	molecular_function	electron transfer activity
C	0016491	molecular_function	oxidoreductase activity
C	0016594	molecular_function	glycine binding
C	0016829	molecular_function	lyase activity
C	0019464	biological_process	glycine decarboxylation via glycine cleavage system
C	0030170	molecular_function	pyridoxal phosphate binding
C	0036255	biological_process	response to methylamine
C	0042803	molecular_function	protein homodimerization activity
C	0070280	molecular_function	pyridoxal binding
C	1903442	biological_process	response to lipoic acid
D	0004375	molecular_function	glycine dehydrogenase (decarboxylating) activity
D	0005739	cellular_component	mitochondrion
D	0005759	cellular_component	mitochondrial matrix
D	0005960	cellular_component	glycine cleavage complex
D	0006520	biological_process	amino acid metabolic process
D	0006544	biological_process	glycine metabolic process
D	0006546	biological_process	glycine catabolic process
D	0009055	molecular_function	electron transfer activity
D	0016491	molecular_function	oxidoreductase activity
D	0016594	molecular_function	glycine binding
D	0016829	molecular_function	lyase activity
D	0019464	biological_process	glycine decarboxylation via glycine cleavage system
D	0030170	molecular_function	pyridoxal phosphate binding
D	0036255	biological_process	response to methylamine
D	0042803	molecular_function	protein homodimerization activity
D	0070280	molecular_function	pyridoxal binding
D	1903442	biological_process	response to lipoic acid

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	binding site for residue PLG A 1101

Chain	Residue
A	TYR161
A	THR653
A	ASP727
A	ALA729
A	ASN751
A	HIS753
A	LYS754
A	GOL1103
A	HOH1210
A	CYS382
A	THR383
A	SER557
A	SER617
A	GLY618
A	ALA619
A	GLU622
A	HIS651

site_id	AC2
Number of Residues	4
Details	binding site for residue EDO A 1102

Chain	Residue
A	ASN543
A	LYS981
A	HOH1380
B	PEG3002

site_id	AC3
Number of Residues	6
Details	binding site for residue GOL A 1103

Chain	Residue
A	TYR164
A	GLN370
A	HIS371
A	HIS651
A	PLG1101
A	HOH1303

site_id	AC4
Number of Residues	9
Details	binding site for residue GOL A 1104

Chain	Residue
A	HIS60
A	ASP61
A	ARG66
A	GLU113
A	ASN114
A	HOH1224
A	HOH1336
B	HIS399
B	HOH3263

site_id	AC5
Number of Residues	2
Details	binding site for residue BCT A 1105

Chain	Residue
A	ARG461
A	LEU462

site_id	AC6
Number of Residues	1
Details	binding site for residue EDO B 3001

Chain	Residue
B	HIS399

site_id	AC7
Number of Residues	6
Details	binding site for residue PEG B 3002

Chain	Residue
A	ASN543
A	EDO1102
A	HOH1363
B	ASN543
B	LYS981
B	PHE982

site_id	AC8
Number of Residues	17
Details	binding site for residue PLG B 3003

Chain	Residue
B	TYR161
B	TYR164
B	CYS382
B	THR383
B	SER557
B	SER617
B	GLY618
B	ALA619
B	GLU622
B	HIS651
B	THR653
B	ASP727
B	ALA729
B	ASN751
B	HIS753
B	LYS754
B	HOH3115

site_id	AC9
Number of Residues	8
Details	binding site for residue GOL B 3004

Chain	Residue
A	HIS399
B	HIS60
B	ASP61
B	ARG66
B	GLU113
B	ASN114
B	HOH3140
B	HOH3149

site_id	AD1
Number of Residues	17
Details	binding site for residue PLG C 1101

Chain	Residue
C	TYR161
C	TYR164
C	CYS382
C	THR383
C	SER557
C	GLY618
C	ALA619
C	GLU622
C	HIS651
C	THR653
C	ASP727
C	ALA729
C	ASN751
C	HIS753
C	LYS754
C	GOL1103
C	HOH1247

site_id	AD2
Number of Residues	2
Details	binding site for residue EDO C 1102

Chain	Residue
C	ARG66
D	HIS399

site_id	AD3
Number of Residues	6
Details	binding site for residue GOL C 1103

Chain	Residue
C	TYR164
C	GLN370
C	HIS371
C	HIS651
C	PLG1101
C	HOH1250

site_id	AD4
Number of Residues	5
Details	binding site for residue PEG C 1104

Chain	Residue
C	HOH1241
C	MET136
C	ARG461
C	LEU462
C	VAL785

site_id	AD5
Number of Residues	7
Details	binding site for residue GOL C 1105

Chain	Residue
C	HIS60
C	ARG66
C	GLU113
C	ASN114
C	HOH1302
C	HOH1322
D	HIS399

site_id	AD6
Number of Residues	7
Details	binding site for residue PEG C 1106

Chain	Residue
C	ASN980
C	LYS981
C	PHE982
C	HOH1449
D	ASN543
D	PEG1103
D	HOH1330

site_id	AD7
Number of Residues	16
Details	binding site for residue PLG D 1101

Chain	Residue
D	TYR161
D	TYR164
D	CYS382
D	THR383
D	SER557
D	GLY618
D	ALA619
D	GLU622
D	HIS651
D	THR653
D	ASP727
D	ALA729
D	ASN751
D	HIS753
D	LYS754
D	HOH1276

site_id	AD8
Number of Residues	4
Details	binding site for residue EDO D 1102

Chain	Residue
C	HIS399
D	HIS60
D	ARG66
D	GLU113

site_id	AD9
Number of Residues	7
Details	binding site for residue PEG D 1103

Chain	Residue
C	PEG1106
D	ASN543
D	LYS981
D	PHE982
D	TRP983
D	THR985
D	HOH1203

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	16
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q91W43","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"UniProtKB","id":"P15505","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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