8CAT

The NADPH binding site on beef liver catalase

Replaces:  3CATReplaces:  1CAT

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004096	molecular_function	catalase activity
A	0004601	molecular_function	peroxidase activity
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005777	cellular_component	peroxisome
A	0006979	biological_process	response to oxidative stress
A	0016491	molecular_function	oxidoreductase activity
A	0019899	molecular_function	enzyme binding
A	0020037	molecular_function	heme binding
A	0042542	biological_process	response to hydrogen peroxide
A	0042744	biological_process	hydrogen peroxide catabolic process
A	0046872	molecular_function	metal ion binding
A	0051781	biological_process	positive regulation of cell division
A	0061692	biological_process	cellular detoxification of hydrogen peroxide
A	0062151	cellular_component	catalase complex
B	0004096	molecular_function	catalase activity
B	0004601	molecular_function	peroxidase activity
B	0005737	cellular_component	cytoplasm
B	0005739	cellular_component	mitochondrion
B	0005777	cellular_component	peroxisome
B	0006979	biological_process	response to oxidative stress
B	0016491	molecular_function	oxidoreductase activity
B	0019899	molecular_function	enzyme binding
B	0020037	molecular_function	heme binding
B	0042542	biological_process	response to hydrogen peroxide
B	0042744	biological_process	hydrogen peroxide catabolic process
B	0046872	molecular_function	metal ion binding
B	0051781	biological_process	positive regulation of cell division
B	0061692	biological_process	cellular detoxification of hydrogen peroxide
B	0062151	cellular_component	catalase complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	23
Details	BINDING SITE FOR RESIDUE HEM A 507

Chain	Residue
A	ARG71
A	ALA157
A	PHE160
A	SER216
A	LEU298
A	PHE333
A	ARG353
A	ALA356
A	TYR357
A	THR360
A	HIS361
A	VAL72
A	ARG364
A	HOH509
A	HOH511
B	ASP64
A	VAL73
A	HIS74
A	ARG111
A	GLY130
A	VAL145
A	GLY146
A	ASN147

---

site_id	AC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE NDP A 508

Chain	Residue
A	HIS193
A	PHE197
A	SER200
A	ARG202
A	LYS236
A	ILE241
A	VAL301
A	TRP302
A	PRO303
A	HIS304
A	GLN441
A	THR444
A	PHE445
A	VAL449
A	HOH512

---

site_id	AC3
Number of Residues	23
Details	BINDING SITE FOR RESIDUE HEM B 507

Chain	Residue
A	ASP64
B	ARG71
B	VAL72
B	VAL73
B	HIS74
B	ARG111
B	GLY130
B	VAL145
B	GLY146
B	ASN147
B	ALA157
B	PHE160
B	GLY215
B	PHE333
B	MET349
B	ARG353
B	ALA356
B	TYR357
B	THR360
B	HIS361
B	ARG364
B	HOH518
B	HOH520

---

site_id	AC4
Number of Residues	15
Details	BINDING SITE FOR RESIDUE NDP B 508

Chain	Residue
B	HIS193
B	PHE197
B	SER200
B	ARG202
B	HIS234
B	LYS236
B	ILE241
B	VAL301
B	TRP302
B	PRO303
B	HIS304
B	GLN441
B	PHE445
B	VAL449
B	HOH521

---

Functional Information from PROSITE/UniProt

site_id	PS00437
Number of Residues	9
Details	CATALASE_1 Catalase proximal heme-ligand signature. RLFAYpDTH

Chain	Residue	Details
A	ARG353-HIS361

---

site_id	PS00438
Number of Residues	17
Details	CATALASE_2 Catalase proximal active site signature. FdReripERvvHakGAG

Chain	Residue	Details
A	PHE63-GLY79

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10013, ECO:0000269|PubMed:7328661

Chain	Residue	Details
A	ALA75
B	ALA75

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10013

Chain	Residue	Details
A	ASN148
B	ASN148

---

site_id	SWS_FT_FI3
Number of Residues	22
Details	BINDING: BINDING => ECO:0000269|PubMed:10417406, ECO:0007744|PDB:4BLC

Chain	Residue	Details
A	GLN194
A	PHE445
A	TYR446
B	GLN194
B	LEU198
B	ASP201
B	GLY203
B	GLY215
B	THR237
B	PRO303
B	GLY305
A	LEU198
B	VAL442
B	PHE445
B	TYR446
A	ASP201
A	GLY203
A	GLY215
A	THR237
A	PRO303
A	GLY305
A	VAL442

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P04040

Chain	Residue	Details
A	GLY213
B	GLY213

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	BINDING: axial binding residue => ECO:0000269|PubMed:10417406, ECO:0007744|PDB:4BLC

Chain	Residue	Details
A	PRO358
B	PRO358

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: N-acetylalanine; alternate => ECO:0000250|UniProtKB:P04040

Chain	Residue	Details
A	ASP2
B	ASP2

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P04040

Chain	Residue	Details
A	ASP9
B	ASP9

---

site_id	SWS_FT_FI8
Number of Residues	4
Details	MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P24270

Chain	Residue	Details
A	HIS13
A	LEU221
B	HIS13
B	LEU221

---

site_id	SWS_FT_FI9
Number of Residues	4
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P24270

Chain	Residue	Details
A	PHE233
A	TYR499
B	PHE233
B	TYR499

---

site_id	SWS_FT_FI10
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P24270

Chain	Residue	Details
A	ALA417
A	ALA434
B	ALA417
B	ALA434

---

site_id	SWS_FT_FI11
Number of Residues	4
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P24270

Chain	Residue	Details
A	VAL449
A	ASN480
B	VAL449
B	ASN480

---