Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4KYO

Alanine-glyoxylate aminotransferase variant K390A in complex with the TPR domain of human Pex5p

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	0007219	biological_process	Notch signaling pathway
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
A	0046724	biological_process	oxalic acid secretion
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	0007219	biological_process	Notch signaling pathway
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
C	0046724	biological_process	oxalic acid secretion

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 A 401

Chain	Residue
A	TYR260
A	THR263
A	HOH629
A	HOH710
C	SER81
C	GLY82
C	HIS83
C	GLN208

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 402

Chain	Residue
A	GLY82
A	HIS83
A	GLN208
C	TYR260
C	THR263
A	SER81

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE BTB A 403

Chain	Residue
A	LYS245
A	TRP246
A	ASN249
A	ASP254
A	GLN256
A	MET259
A	HOH528
A	HOH566

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE BME A 404

Chain	Residue
A	HIS155
A	GLN164
A	LEU166
A	PRO192
A	GLN198
A	HOH516

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE BME A 405

Chain	Residue
A	MET348
A	GLY349
A	GLY350

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE BME A 406

Chain	Residue
A	TYR297
C	ASP167
C	GLY168
C	HOH558

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE BME A 407

Chain	Residue
A	PRO125
A	MET126
A	THR127

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE BME A 408

Chain	Residue
A	PRO265
A	VAL266
A	ILE267
A	SER268
C	PRO214
C	PRO215
C	SER268

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE BTB C 401

Chain	Residue
C	LYS245
C	TRP246
C	ASN249
C	ASP254
C	GLN256
C	MET259

site_id	BC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE BME C 402

Chain	Residue
C	VAL77
C	ILE78
C	SER79
C	TYR241
C	LEU247
C	TRP251
C	HIS262

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE BME C 403

Chain	Residue
C	LYS147
C	PRO148
C	LYS177

site_id	BC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE BME C 404

Chain	Residue
A	SER19
C	ASP52
C	GLU59

site_id	BC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE BME C 405

Chain	Residue
A	ASP52
A	GLN55
C	SER19

site_id	BC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE BME C 406

Chain	Residue
C	TRP332
C	MET348
C	GLY349
C	GLY350
C	ARG360
C	HOH618

site_id	BC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE BME B 701

Chain	Residue
B	ASN520
B	TYR522
B	LEU551
B	GLN552
B	HOH847
D	GLN347
D	LEU551
D	GLN552

site_id	BC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE BME D 701

Chain	Residue
D	LYS527
D	HOH847

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	2
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	2
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine"}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
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	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"O35423","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	66
Details	Repeat: {"description":"TPR 1"}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	66
Details	Repeat: {"description":"TPR 2"}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	66
Details	Repeat: {"description":"TPR 3"}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	66
Details	Repeat: {"description":"TPR 5"}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	66
Details	Repeat: {"description":"TPR 6"}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	66
Details	Repeat: {"description":"TPR 7"}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"28724525","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"24662292","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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