6PM7

The structure of the triclinic crystal form of beef liver catalase at 1.85 A resolution

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	0005782	cellular_component	peroxisomal matrix
A	0006979	biological_process	response to oxidative stress
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	0005782	cellular_component	peroxisomal matrix
B	0006979	biological_process	response to oxidative stress
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	26
Details	binding site for residue HEM A 601

Chain	Residue
A	ARG71
A	ALA157
A	PHE160
A	SER216
A	LEU298
A	PHE333
A	MET349
A	ARG353
A	TYR357
A	THR360
A	HIS361
A	VAL72
A	ARG364
A	HOH724
A	HOH747
A	HOH794
A	HOH860
B	MET60
B	ASP64
A	VAL73
A	HIS74
A	ARG111
A	GLY130
A	VAL145
A	GLY146
A	ASN147

---

site_id	AC2
Number of Residues	19
Details	binding site for residue NDP A 602

Chain	Residue
A	HIS193
A	PHE197
A	SER200
A	ARG202
A	ASP212
A	HIS234
A	LYS236
A	VAL301
A	TRP302
A	PRO303
A	HIS304
A	GLN441
A	THR444
A	PHE445
A	VAL449
A	HOH701
A	HOH760
A	HOH769
A	HOH867

---

site_id	AC3
Number of Residues	25
Details	binding site for residue HEM B 601

Chain	Residue
A	MET60
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	SER216
B	HIS217
B	PHE333
B	MET349
B	ARG353
B	TYR357
B	THR360
B	HIS361
B	ARG364
B	HOH724
B	HOH795
B	HOH803

---

site_id	AC4
Number of Residues	21
Details	binding site for residue NDP B 602

Chain	Residue
B	HIS193
B	PHE197
B	SER200
B	ARG202
B	ASP212
B	HIS234
B	LYS236
B	VAL301
B	TRP302
B	PRO303
B	HIS304
B	GLN441
B	THR444
B	PHE445
B	VAL449
B	LEU450
B	HOH711
B	HOH759
B	HOH790
B	HOH879
B	HOH942

---

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	HIS74
B	HIS74

---

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

Chain	Residue	Details
A	ASN147
B	ASN147

---

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

Chain	Residue	Details
A	HIS193
A	THR444
A	PHE445
B	HIS193
B	PHE197
B	SER200
B	ARG202
B	TYR214
B	LYS236
B	TRP302
B	HIS304
A	PHE197
B	GLN441
B	THR444
B	PHE445
A	SER200
A	ARG202
A	TYR214
A	LYS236
A	TRP302
A	HIS304
A	GLN441

---

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

Chain	Residue	Details
A	ASP212
B	ASP212

---

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	TYR357
B	TYR357

---

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

Chain	Residue	Details
A	ALA1
B	ALA1

---

site_id	SWS_FT_FI7
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P04040

Chain	Residue	Details
A	SER8
A	SER516
B	SER8
B	SER516

---

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

Chain	Residue	Details
A	LYS12
A	LYS220
B	LYS12
B	LYS220

---

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

Chain	Residue	Details
A	LYS232
A	LYS498
B	LYS232
B	LYS498

---

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

Chain	Residue	Details
A	SER416
A	SER433
B	SER416
B	SER433

---

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

Chain	Residue	Details
A	LYS448
A	LYS479
B	LYS448
B	LYS479

---

site_id	SWS_FT_FI12
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P04040

Chain	Residue	Details
A	THR510
B	THR510

---