Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4I8A

Alanine-glyoxylate aminotransferase variant S187F

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004760	molecular_function	L-serine-pyruvate transaminase activity
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005777	cellular_component	peroxisome
A	0005782	cellular_component	peroxisomal matrix
A	0005829	cellular_component	cytosol
A	0006563	biological_process	L-serine metabolic process
A	0008453	molecular_function	alanine-glyoxylate transaminase activity
A	0008483	molecular_function	transaminase activity
A	0009436	biological_process	glyoxylate catabolic process
A	0016597	molecular_function	amino acid binding
A	0016740	molecular_function	transferase activity
A	0019265	biological_process	glycine biosynthetic process, by transamination of glyoxylate
A	0019448	biological_process	L-cysteine catabolic process
A	0030170	molecular_function	pyridoxal phosphate binding
A	0042802	molecular_function	identical protein binding
A	0042803	molecular_function	protein homodimerization activity
A	0042853	biological_process	L-alanine catabolic process
A	0046487	biological_process	glyoxylate metabolic process
B	0004760	molecular_function	L-serine-pyruvate transaminase activity
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0005777	cellular_component	peroxisome
B	0005782	cellular_component	peroxisomal matrix
B	0005829	cellular_component	cytosol
B	0006563	biological_process	L-serine metabolic process
B	0008453	molecular_function	alanine-glyoxylate transaminase activity
B	0008483	molecular_function	transaminase activity
B	0009436	biological_process	glyoxylate catabolic process
B	0016597	molecular_function	amino acid binding
B	0016740	molecular_function	transferase activity
B	0019265	biological_process	glycine biosynthetic process, by transamination of glyoxylate
B	0019448	biological_process	L-cysteine catabolic process
B	0030170	molecular_function	pyridoxal phosphate binding
B	0042802	molecular_function	identical protein binding
B	0042803	molecular_function	protein homodimerization activity
B	0042853	biological_process	L-alanine catabolic process
B	0046487	biological_process	glyoxylate metabolic process
C	0004760	molecular_function	L-serine-pyruvate transaminase activity
C	0005515	molecular_function	protein binding
C	0005737	cellular_component	cytoplasm
C	0005777	cellular_component	peroxisome
C	0005782	cellular_component	peroxisomal matrix
C	0005829	cellular_component	cytosol
C	0006563	biological_process	L-serine metabolic process
C	0008453	molecular_function	alanine-glyoxylate transaminase activity
C	0008483	molecular_function	transaminase activity
C	0009436	biological_process	glyoxylate catabolic process
C	0016597	molecular_function	amino acid binding
C	0016740	molecular_function	transferase activity
C	0019265	biological_process	glycine biosynthetic process, by transamination of glyoxylate
C	0019448	biological_process	L-cysteine catabolic process
C	0030170	molecular_function	pyridoxal phosphate binding
C	0042802	molecular_function	identical protein binding
C	0042803	molecular_function	protein homodimerization activity
C	0042853	biological_process	L-alanine catabolic process
C	0046487	biological_process	glyoxylate metabolic process
D	0004760	molecular_function	L-serine-pyruvate transaminase activity
D	0005515	molecular_function	protein binding
D	0005737	cellular_component	cytoplasm
D	0005777	cellular_component	peroxisome
D	0005782	cellular_component	peroxisomal matrix
D	0005829	cellular_component	cytosol
D	0006563	biological_process	L-serine metabolic process
D	0008453	molecular_function	alanine-glyoxylate transaminase activity
D	0008483	molecular_function	transaminase activity
D	0009436	biological_process	glyoxylate catabolic process
D	0016597	molecular_function	amino acid binding
D	0016740	molecular_function	transferase activity
D	0019265	biological_process	glycine biosynthetic process, by transamination of glyoxylate
D	0019448	biological_process	L-cysteine catabolic process
D	0030170	molecular_function	pyridoxal phosphate binding
D	0042802	molecular_function	identical protein binding
D	0042803	molecular_function	protein homodimerization activity
D	0042853	biological_process	L-alanine catabolic process
D	0046487	biological_process	glyoxylate metabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 401

Chain	Residue
A	GLY29
A	LEU351
A	ARG360
B	SER48

site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL A 402

Chain	Residue
A	GLN110
A	ARG111

site_id	AC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE GOL B 401

Chain	Residue
B	LYS51

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL B 402

Chain	Residue
B	PRO28
B	GLY29
B	LEU351
B	ARG360
A	MET49
A	TYR260

site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL C 401

Chain	Residue
C	HIS133
C	THR135

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL C 402

Chain	Residue
A	PRO130
A	PHE310
A	LYS357
C	HIS124
C	PRO125
C	HIS146

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL C 403

Chain	Residue
C	MET348
C	ARG360
D	MET49
D	TYR260

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL C 404

Chain	Residue
C	GLY283
C	GLU285
C	ASN286

site_id	AC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL D 401

Chain	Residue
D	ARG122
D	HIS124

site_id	BC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL D 402

Chain	Residue
D	PRO73
D	GOL404

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL D 403

Chain	Residue
B	LYS228
D	ASP255
D	GOL404

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL D 404

Chain	Residue
D	LYS227
D	CYS253
D	GOL402
D	GOL403

site_id	BC4
Number of Residues	1
Details	BINDING SITE FOR RESIDUE GOL D 405

Chain	Residue
D	GLU138

Functional Information from PROSITE/UniProt

site_id	PS00595
Number of Residues	21
Details	AA_TRANSFER_CLASS_5 Aminotransferases class-V pyridoxal-phosphate attachment site. IDILysGSQKalnappGtSlI

Chain	Residue	Details
A	ILE200-ILE220

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine"}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"O35423","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	8
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"O35423","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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