Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3PCH

STRUCTURE OF PROTOCATECHUATE 3,4-DIOXYGENASE COMPLEXED WITH 3-CHLORO-4-HYDROXYBENZOATE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0005506	molecular_function	iron ion binding
A	0008199	molecular_function	ferric iron binding
A	0009056	biological_process	catabolic process
A	0016702	molecular_function	oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
A	0018578	molecular_function	protocatechuate 3,4-dioxygenase activity
A	0042952	biological_process	beta-ketoadipate pathway
A	0051213	molecular_function	dioxygenase activity
B	0003824	molecular_function	catalytic activity
B	0005506	molecular_function	iron ion binding
B	0008199	molecular_function	ferric iron binding
B	0009056	biological_process	catabolic process
B	0016702	molecular_function	oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
B	0018578	molecular_function	protocatechuate 3,4-dioxygenase activity
B	0042952	biological_process	beta-ketoadipate pathway
B	0051213	molecular_function	dioxygenase activity
C	0003824	molecular_function	catalytic activity
C	0005506	molecular_function	iron ion binding
C	0008199	molecular_function	ferric iron binding
C	0009056	biological_process	catabolic process
C	0016702	molecular_function	oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
C	0018578	molecular_function	protocatechuate 3,4-dioxygenase activity
C	0042952	biological_process	beta-ketoadipate pathway
C	0051213	molecular_function	dioxygenase activity
D	0003824	molecular_function	catalytic activity
D	0005506	molecular_function	iron ion binding
D	0008199	molecular_function	ferric iron binding
D	0009056	biological_process	catabolic process
D	0016702	molecular_function	oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
D	0018578	molecular_function	protocatechuate 3,4-dioxygenase activity
D	0042952	biological_process	beta-ketoadipate pathway
D	0051213	molecular_function	dioxygenase activity
E	0003824	molecular_function	catalytic activity
E	0005506	molecular_function	iron ion binding
E	0008199	molecular_function	ferric iron binding
E	0009056	biological_process	catabolic process
E	0016702	molecular_function	oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
E	0018578	molecular_function	protocatechuate 3,4-dioxygenase activity
E	0042952	biological_process	beta-ketoadipate pathway
E	0051213	molecular_function	dioxygenase activity
F	0003824	molecular_function	catalytic activity
F	0005506	molecular_function	iron ion binding
F	0008199	molecular_function	ferric iron binding
F	0009056	biological_process	catabolic process
F	0016702	molecular_function	oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
F	0018578	molecular_function	protocatechuate 3,4-dioxygenase activity
F	0042952	biological_process	beta-ketoadipate pathway
F	0051213	molecular_function	dioxygenase activity
M	0003824	molecular_function	catalytic activity
M	0005506	molecular_function	iron ion binding
M	0008199	molecular_function	ferric iron binding
M	0009056	biological_process	catabolic process
M	0016702	molecular_function	oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
M	0018578	molecular_function	protocatechuate 3,4-dioxygenase activity
M	0019619	biological_process	3,4-dihydroxybenzoate catabolic process
M	0042952	biological_process	beta-ketoadipate pathway
M	0046872	molecular_function	metal ion binding
M	0051213	molecular_function	dioxygenase activity
N	0003824	molecular_function	catalytic activity
N	0005506	molecular_function	iron ion binding
N	0008199	molecular_function	ferric iron binding
N	0009056	biological_process	catabolic process
N	0016702	molecular_function	oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
N	0018578	molecular_function	protocatechuate 3,4-dioxygenase activity
N	0019619	biological_process	3,4-dihydroxybenzoate catabolic process
N	0042952	biological_process	beta-ketoadipate pathway
N	0046872	molecular_function	metal ion binding
N	0051213	molecular_function	dioxygenase activity
O	0003824	molecular_function	catalytic activity
O	0005506	molecular_function	iron ion binding
O	0008199	molecular_function	ferric iron binding
O	0009056	biological_process	catabolic process
O	0016702	molecular_function	oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
O	0018578	molecular_function	protocatechuate 3,4-dioxygenase activity
O	0019619	biological_process	3,4-dihydroxybenzoate catabolic process
O	0042952	biological_process	beta-ketoadipate pathway
O	0046872	molecular_function	metal ion binding
O	0051213	molecular_function	dioxygenase activity
P	0003824	molecular_function	catalytic activity
P	0005506	molecular_function	iron ion binding
P	0008199	molecular_function	ferric iron binding
P	0009056	biological_process	catabolic process
P	0016702	molecular_function	oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
P	0018578	molecular_function	protocatechuate 3,4-dioxygenase activity
P	0019619	biological_process	3,4-dihydroxybenzoate catabolic process
P	0042952	biological_process	beta-ketoadipate pathway
P	0046872	molecular_function	metal ion binding
P	0051213	molecular_function	dioxygenase activity
Q	0003824	molecular_function	catalytic activity
Q	0005506	molecular_function	iron ion binding
Q	0008199	molecular_function	ferric iron binding
Q	0009056	biological_process	catabolic process
Q	0016702	molecular_function	oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
Q	0018578	molecular_function	protocatechuate 3,4-dioxygenase activity
Q	0019619	biological_process	3,4-dihydroxybenzoate catabolic process
Q	0042952	biological_process	beta-ketoadipate pathway
Q	0046872	molecular_function	metal ion binding
Q	0051213	molecular_function	dioxygenase activity
R	0003824	molecular_function	catalytic activity
R	0005506	molecular_function	iron ion binding
R	0008199	molecular_function	ferric iron binding
R	0009056	biological_process	catabolic process
R	0016702	molecular_function	oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
R	0018578	molecular_function	protocatechuate 3,4-dioxygenase activity
R	0019619	biological_process	3,4-dihydroxybenzoate catabolic process
R	0042952	biological_process	beta-ketoadipate pathway
R	0046872	molecular_function	metal ion binding
R	0051213	molecular_function	dioxygenase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FE M 600

Chain	Residue
M	TYR408
M	TYR447
M	HIS460
M	HIS462
M	CHB550
M	HOH742

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FE N 600

Chain	Residue
N	TYR408
N	TYR447
N	HIS460
N	HIS462
N	CHB550
N	HOH846

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FE O 600

Chain	Residue
O	TYR408
O	TYR447
O	HIS460
O	HIS462
O	CHB550
O	HOH861

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FE P 600

Chain	Residue
P	TYR408
P	TYR447
P	HIS460
P	HIS462
P	CHB550
P	HOH778

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FE Q 600

Chain	Residue
Q	TYR408
Q	TYR447
Q	HIS460
Q	HIS462
Q	CHB550
Q	HOH774

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FE R 600

Chain	Residue
R	TYR408
R	TYR447
R	HIS460
R	HIS462
R	CHB550
R	HOH861

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE BME M 601

Chain	Residue
M	HIS361
M	CYS429
M	SER438
M	HOH691

site_id	AC8
Number of Residues	14
Details	BINDING SITE FOR RESIDUE CHB M 550

Chain	Residue
A	THR12
A	GLY14
A	PRO15
A	ARG133
M	TYR324
M	TYR447
M	TRP449
M	ARG457
M	HIS460
M	HIS462
M	GLN477
M	ILE491
M	FE600
M	HOH742

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CHB M 551

Chain	Residue
M	ARG333
M	HOH680
M	HOH736
M	HOH746
O	ILE328

site_id	ACA
Number of Residues	28
Details	SITE "ACA" IS THE ACTIVE SITE OF THE PROTOMER CONSISTING OF CHAINS A AND M.

Chain	Residue
A	THR12
M	TRP400
M	TYR408
M	TYR447
M	PRO448
M	TRP449
M	ARG450
M	ARG457
M	HIS460
M	HIS462
M	GLN477
A	ALA13
M	ILE491
M	CHB550
M	FE600
M	HOH605
A	HOH606
M	HOH625
M	HOH633
M	HOH634
M	HOH742
A	GLY14
A	PRO15
A	TYR16
A	ARG133
A	GLY134
M	TYR324
M	THR326

site_id	ACB
Number of Residues	28
Details	SITE "ACB" IS THE ACTIVE SITE OF THE PROTOMER CONSISTING OF CHAINS B AND N.

Chain	Residue
B	THR12
B	ALA13
B	GLY14
B	PRO15
B	TYR16
B	ARG133
B	GLY134
N	TYR324
N	THR326
N	TRP400
N	TYR408
N	TYR447
N	PRO448
N	TRP449
N	ARG450
N	ARG457
N	HIS460
N	HIS462
N	GLN477
N	ILE491
N	CHB550
N	FE600
N	HOH699
B	HOH606
N	HOH721
N	HOH729
N	HOH730
N	HOH846

site_id	ACC
Number of Residues	28
Details	SITE "ACC" IS THE ACTIVE SITE OF THE PROTOMER CONSISTING OF CHAINS C AND O.

Chain	Residue
C	THR12
C	ALA13
C	GLY14
C	PRO15
C	TYR16
C	ARG133
C	GLY134
O	TYR324
O	THR326
O	TRP400
O	TYR408
O	TYR447
O	PRO448
O	TRP449
O	ARG450
O	ARG457
O	HIS460
O	HIS462
O	GLN477
O	ILE491
O	CHB550
O	FE600
O	HOH605
C	HOH606
O	HOH643
O	HOH659
O	HOH660
O	HOH861

site_id	ACD
Number of Residues	28
Details	SITE "ACD" IS THE ACTIVE SITE OF THE PROTOMER CONSISTING OF CHAINS D AND P.

Chain	Residue
P	ARG457
P	HIS460
P	HIS462
P	GLN477
P	ILE491
P	CHB550
P	FE600
D	HOH605
D	HOH606
P	HOH666
P	HOH674
P	HOH675
P	HOH778
D	THR12
D	ALA13
D	GLY14
D	PRO15
D	TYR16
D	ARG133
D	GLY134
P	TYR324
P	THR326
P	TRP400
P	TYR408
P	TYR447
P	PRO448
P	TRP449
P	ARG450

site_id	ACE
Number of Residues	28
Details	SITE "ACE" IS THE ACTIVE SITE OF THE PROTOMER CONSISTING OF CHAINS E AND Q.

Chain	Residue
E	THR12
E	ALA13
E	GLY14
E	PRO15
E	TYR16
E	ARG133
E	GLY134
Q	TYR324
Q	THR326
Q	TRP400
Q	TYR408
Q	TYR447
Q	PRO448
Q	TRP449
Q	ARG450
Q	ARG457
Q	HIS460
Q	HIS462
Q	GLN477
Q	ILE491
Q	CHB550
Q	FE600
Q	HOH626
E	HOH606
Q	HOH651
Q	HOH659
Q	HOH660
Q	HOH774

site_id	ACF
Number of Residues	28
Details	SITE "ACF" IS THE ACTIVE SITE OF THE PROTOMER CONSISTING OF CHAINS F AND R.

Chain	Residue
F	THR12
F	ALA13
F	GLY14
F	PRO15
F	TYR16
F	ARG133
F	GLY134
R	TYR324
R	THR326
R	TRP400
R	TYR408
R	TYR447
R	PRO448
R	TRP449
R	ARG450
R	ARG457
R	HIS460
R	HIS462
R	GLN477
R	ILE491
R	CHB550
R	FE600
R	HOH605
F	HOH606
R	HOH643
R	HOH659
R	HOH660
R	HOH861

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE BME N 601

Chain	Residue
N	HIS361
N	CYS429
N	LEU430
N	SER438

site_id	BC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE CHB N 550

Chain	Residue
B	THR12
B	PRO15
B	ARG133
N	TYR324
N	TYR408
N	TYR447
N	TRP449
N	ARG457
N	HIS460
N	HIS462
N	GLN477
N	ILE491
N	FE600
N	HOH846

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CHB N 551

Chain	Residue
M	PRO322
M	ILE328
M	HOH749
N	ARG333
N	HOH777
N	HOH840

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE BME O 601

Chain	Residue
O	HIS361
O	CYS429
O	SER438
O	HOH751

site_id	BC5
Number of Residues	14
Details	BINDING SITE FOR RESIDUE CHB O 550

Chain	Residue
C	THR12
C	PRO15
C	ARG133
O	TYR324
O	TYR408
O	TYR447
O	TRP449
O	ARG457
O	HIS460
O	HIS462
O	GLN477
O	ILE491
O	FE600
O	HOH861

site_id	BC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CHB O 551

Chain	Residue
N	PRO322
N	ILE328
O	ARG333
O	HOH732
O	HOH847
O	HOH868

site_id	BC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE BME P 601

Chain	Residue
P	HIS361
P	CYS429
P	LEU430
P	SER438
P	HOH730

site_id	BC8
Number of Residues	14
Details	BINDING SITE FOR RESIDUE CHB P 550

Chain	Residue
D	THR12
D	GLY14
D	PRO15
D	ARG133
P	TYR324
P	TYR447
P	TRP449
P	ARG457
P	HIS460
P	HIS462
P	GLN477
P	ILE491
P	FE600
P	HOH778

site_id	BC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CHB P 551

Chain	Residue
P	ARG333
P	HOH719
P	HOH772
P	HOH781
R	PRO322
R	ILE328

site_id	CC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE BME Q 601

Chain	Residue
Q	HIS361
Q	CYS429
Q	LEU430
Q	SER438
Q	HOH719

site_id	CC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE CHB Q 550

Chain	Residue
E	THR12
E	GLY14
E	PRO15
Q	TYR324
Q	TYR408
Q	TYR447
Q	TRP449
Q	ARG457
Q	HIS460
Q	HIS462
Q	GLN477
Q	ILE491
Q	FE600
Q	HOH774

site_id	CC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CHB Q 551

Chain	Residue
P	ILE328
Q	ARG333
Q	HOH708
Q	HOH768
Q	HOH779

site_id	CC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE BME R 601

Chain	Residue
R	HIS361
R	CYS429
R	LEU430
R	SER438
R	HOH751

site_id	CC5
Number of Residues	14
Details	BINDING SITE FOR RESIDUE CHB R 550

Chain	Residue
F	THR12
F	PRO15
F	ARG133
R	TYR324
R	TYR408
R	TYR447
R	TRP449
R	ARG457
R	HIS460
R	HIS462
R	GLN477
R	ILE491
R	FE600
R	HOH861

site_id	CC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CHB R 551

Chain	Residue
Q	PRO322
Q	ILE328
R	ARG333
R	HOH732
R	HOH847
R	HOH868

site_id	S2M
Number of Residues	45
Details	SECONDARY THREE-FOLD SITE BETWEEN M, N, O CHAINS.

Chain	Residue
M	LYS318
M	LEU320
M	PRO322
M	ILE328
M	PRO332
M	ARG333
M	GLN334
M	CHB551
M	HOH680
M	HOH697
M	HOH709
O	HOH846
M	HOH736
M	HOH744
M	HOH746
N	LYS318
N	LEU320
N	PRO322
N	ILE328
N	PRO332
N	ARG333
N	GLN334
N	CHB551
N	HOH777
N	HOH795
N	HOH808
M	HOH748
N	HOH840
N	HOH849
M	HOH749
O	LYS318
O	LEU320
O	PRO322
O	ILE328
O	PRO332
O	ARG333
O	GLN334
O	CHB551
O	HOH732
O	HOH760
O	HOH784
N	HOH853
O	HOH847
O	HOH865
O	HOH868

site_id	S2P
Number of Residues	45
Details	SECONDARY THREE-FOLD SITE BETWEEN P, Q, R CHAINS.

Chain	Residue
P	LYS318
P	LEU320
P	PRO322
P	ILE328
P	PRO332
P	ARG333
P	GLN334
P	CHB551
P	HOH719
P	HOH736
P	HOH747
R	HOH846
P	HOH772
P	HOH779
P	HOH781
Q	LYS318
Q	LEU320
Q	PRO322
Q	ILE328
Q	PRO332
Q	ARG333
Q	GLN334
Q	CHB551
Q	HOH708
Q	HOH725
Q	HOH737
P	HOH783
Q	HOH768
Q	HOH777
Q	HOH779
R	LYS318
R	LEU320
R	PRO322
R	ILE328
R	PRO332
R	ARG333
R	GLN334
R	CHB551
R	HOH732
R	HOH760
R	HOH784
Q	HOH781
R	HOH847
R	HOH865
R	HOH868

site_id	VEA
Number of Residues	29
Details	SITE "VEA" IS THE VESTIGIAL SITE OF THE PROTOMER CONSISTING OF CHAINS A AND M.

Chain	Residue
A	TYR79
A	VAL114
A	ASN115
A	ASN116
A	ALA117
A	ALA118
A	MET122
A	HIS125
A	ASN127
A	ARG142
A	VAL157
M	ASP304
M	ARG307
M	ILE339
M	PRO340
M	GLN341
M	SER342
M	ILE343
M	SER344
M	GLU345
A	HOH646
M	HOH631
M	HOH638
A	HOH673
M	HOH644
A	HOH683
M	HOH660
A	HOH725
N	HOH696

site_id	VEB
Number of Residues	29
Details	SITE "VEB" IS THE VESTIGIAL SITE OF THE PROTOMER CONSISTING OF CHAINS B AND N.

Chain	Residue
B	TYR79
B	VAL114
B	ASN115
B	ASN116
B	ALA117
B	ALA118
B	MET122
B	HIS125
B	ASN127
B	ARG142
B	VAL157
N	ASP304
N	ARG307
N	ILE339
N	PRO340
N	GLN341
N	SER342
N	ILE343
N	SER344
N	GLU345
B	HOH646
N	HOH727
N	HOH734
B	HOH673
N	HOH741
N	HOH743
N	HOH757
N	HOH771
O	HOH795

site_id	VEC
Number of Residues	29
Details	SITE "VEC" IS THE VESTIGIAL SITE OF THE PROTOMER CONSISTING OF CHAINS C AND O.

Chain	Residue
C	TYR79
C	VAL114
C	ASN115
C	ASN116
C	ALA117
C	ALA118
C	MET122
C	HIS125
C	ASN127
C	ARG142
C	VAL157
O	ASP304
O	ARG307
O	ILE339
O	PRO340
O	GLN341
O	SER342
O	ILE343
O	SER344
O	GLU345
C	HOH646
O	HOH655
O	HOH666
C	HOH673
O	HOH681
C	HOH683
O	HOH707
C	HOH725
M	HOH752

site_id	VED
Number of Residues	29
Details	SITE "VED" IS THE VESTIGIAL SITE OF THE PROTOMER CONSISTING OF CHAINS D AND P.

Chain	Residue
D	TYR79
D	VAL114
D	ASN115
D	ASN116
D	ALA117
D	ALA118
D	MET122
D	HIS125
D	ASN127
D	ARG142
D	VAL157
P	ASP304
P	ARG307
P	ILE339
P	PRO340
P	GLN341
P	SER342
P	ILE343
P	SER344
P	GLU345
D	HOH646
P	HOH672
D	HOH666
D	HOH673
P	HOH685
D	HOH683
P	HOH700
D	HOH725
Q	HOH624

site_id	VEE
Number of Residues	29
Details	SITE "VEE" IS THE VESTIGIAL SITE OF THE PROTOMER CONSISTING OF CHAINS E AND Q.

Chain	Residue
E	TYR79
E	VAL114
E	ASN115
E	ASN116
E	ALA117
E	ALA118
E	MET122
E	HIS125
E	ASN127
E	ARG142
E	VAL157
Q	ASP304
Q	ARG307
Q	ILE339
Q	PRO340
Q	GLN341
Q	SER342
Q	ILE343
Q	SER344
Q	GLU345
E	HOH646
E	HOH655
E	HOH666
E	HOH673
Q	HOH672
E	HOH683
Q	HOH687
E	HOH725
R	HOH795

site_id	VEF
Number of Residues	29
Details	SITE "VEF" IS THE VESTIGIAL SITE OF THE PROTOMER CONSISTING OF CHAINS F AND R.

Chain	Residue
F	TYR79
F	VAL114
F	ASN115
F	ASN116
F	ALA117
F	ALA118
F	MET122
F	HIS125
F	ASN127
F	ARG142
F	VAL157
R	ASP304
R	ARG307
R	ILE339
R	PRO340
R	GLN341
R	SER342
R	ILE343
R	SER344
R	GLU345
F	HOH646
R	HOH655
R	HOH666
F	HOH673
R	HOH681
R	HOH683
R	HOH707
R	HOH725
P	HOH786

Functional Information from PROSITE/UniProt

site_id	PS00083
Number of Residues	29
Details	INTRADIOL_DIOXYGENAS Intradiol ring-cleavage dioxygenases signature. VaGrVvdqyGkpVpntlVEMwqanagGrY

Chain	Residue	Details
M	VAL380-TYR408
A	LEU51-TYR79

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	BINDING: BINDING => ECO:0000269\|PubMed:7990141

Chain	Residue	Details
M	ARG409
O	PRO448
O	ILE461
O	PHE463
P	ARG409
P	PRO448
P	ILE461
P	PHE463
Q	ARG409
Q	PRO448
Q	ILE461
M	PRO448
Q	PHE463
R	ARG409
R	PRO448
R	ILE461
R	PHE463
M	ILE461
M	PHE463
N	ARG409
N	PRO448
N	ILE461
N	PHE463
O	ARG409

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 3pca

Chain	Residue	Details
M	TYR447
M	ARG457

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 3pca

Chain	Residue	Details
N	TYR447
N	ARG457

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 3pca

Chain	Residue	Details
O	TYR447
O	ARG457

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 3pca

Chain	Residue	Details
P	TYR447
P	ARG457

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 3pca

Chain	Residue	Details
Q	TYR447
Q	ARG457

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 3pca

Chain	Residue	Details
R	TYR447
R	ARG457

site_id	MCSA1
Number of Residues	5
Details	M-CSA 936

Chain	Residue	Details
M	ARG409	metal ligand
M	PRO448	metal ligand, proton shuttle (general acid/base)
M	PRO458	electrostatic stabiliser
M	ILE461	metal ligand
M	PHE463	metal ligand

site_id	MCSA2
Number of Residues	5
Details	M-CSA 936

Chain	Residue	Details
N	ARG409	metal ligand
N	PRO448	metal ligand, proton shuttle (general acid/base)
N	PRO458	electrostatic stabiliser
N	ILE461	metal ligand
N	PHE463	metal ligand

site_id	MCSA3
Number of Residues	5
Details	M-CSA 936

Chain	Residue	Details
O	ARG409	metal ligand
O	PRO448	metal ligand, proton shuttle (general acid/base)
O	PRO458	electrostatic stabiliser
O	ILE461	metal ligand
O	PHE463	metal ligand

site_id	MCSA4
Number of Residues	5
Details	M-CSA 936

Chain	Residue	Details
P	ARG409	metal ligand
P	PRO448	metal ligand, proton shuttle (general acid/base)
P	PRO458	electrostatic stabiliser
P	ILE461	metal ligand
P	PHE463	metal ligand

site_id	MCSA5
Number of Residues	5
Details	M-CSA 936

Chain	Residue	Details
Q	ARG409	metal ligand
Q	PRO448	metal ligand, proton shuttle (general acid/base)
Q	PRO458	electrostatic stabiliser
Q	ILE461	metal ligand
Q	PHE463	metal ligand

site_id	MCSA6
Number of Residues	5
Details	M-CSA 936

Chain	Residue	Details
R	ARG409	metal ligand
R	PRO448	metal ligand, proton shuttle (general acid/base)
R	PRO458	electrostatic stabiliser
R	ILE461	metal ligand
R	PHE463	metal ligand

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)