Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5GYR

Tetrameric Allochromatium vinosum cytochrome c'

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005506	molecular_function	iron ion binding
A	0009055	molecular_function	electron transfer activity
A	0020037	molecular_function	heme binding
A	0022900	biological_process	electron transport chain
A	0042597	cellular_component	periplasmic space
A	0046872	molecular_function	metal ion binding
B	0005506	molecular_function	iron ion binding
B	0009055	molecular_function	electron transfer activity
B	0020037	molecular_function	heme binding
B	0022900	biological_process	electron transport chain
B	0042597	cellular_component	periplasmic space
B	0046872	molecular_function	metal ion binding
E	0005506	molecular_function	iron ion binding
E	0009055	molecular_function	electron transfer activity
E	0020037	molecular_function	heme binding
E	0022900	biological_process	electron transport chain
E	0042597	cellular_component	periplasmic space
E	0046872	molecular_function	metal ion binding
F	0005506	molecular_function	iron ion binding
F	0009055	molecular_function	electron transfer activity
F	0020037	molecular_function	heme binding
F	0022900	biological_process	electron transport chain
F	0042597	cellular_component	periplasmic space
F	0046872	molecular_function	metal ion binding
I	0005506	molecular_function	iron ion binding
I	0009055	molecular_function	electron transfer activity
I	0020037	molecular_function	heme binding
I	0022900	biological_process	electron transport chain
I	0042597	cellular_component	periplasmic space
I	0046872	molecular_function	metal ion binding
J	0005506	molecular_function	iron ion binding
J	0009055	molecular_function	electron transfer activity
J	0020037	molecular_function	heme binding
J	0022900	biological_process	electron transport chain
J	0042597	cellular_component	periplasmic space
J	0046872	molecular_function	metal ion binding
M	0005506	molecular_function	iron ion binding
M	0009055	molecular_function	electron transfer activity
M	0020037	molecular_function	heme binding
M	0022900	biological_process	electron transport chain
M	0042597	cellular_component	periplasmic space
M	0046872	molecular_function	metal ion binding
N	0005506	molecular_function	iron ion binding
N	0009055	molecular_function	electron transfer activity
N	0020037	molecular_function	heme binding
N	0022900	biological_process	electron transport chain
N	0042597	cellular_component	periplasmic space
N	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	binding site for residue HEC A 201

Chain	Residue
A	PHE91
N	GLY20
N	TYR58
N	THR71
N	ARG72
A	CYS121
A	CYS124
A	HIS125
A	ARG129
A	HOH310
N	ARG12
N	GLN13
N	TYR16

site_id	AC2
Number of Residues	17
Details	binding site for Di-peptide HEM B 201 and CYS B 124

Chain	Residue
B	ARG12
B	GLN13
B	TYR16
B	TYR58
B	THR71
B	ARG72
B	PHE91
B	ALA120
B	CYS121
B	LYS122
B	SER123
B	HIS125
B	GLU126
B	LYS127
B	TYR128
B	ARG129
B	HOH306

site_id	AC3
Number of Residues	17
Details	binding site for Di-peptide HEM B 201 and CYS B 121

Chain	Residue
B	ARG12
B	GLN13
B	TYR16
B	TYR58
B	THR71
B	ARG72
B	PHE91
B	VAL117
B	GLY118
B	ALA119
B	ALA120
B	LYS122
B	SER123
B	CYS124
B	HIS125
B	ARG129
B	HOH306

site_id	AC4
Number of Residues	18
Details	binding site for Di-peptide HEM E 201 and CYS E 124

Chain	Residue
E	PHE91
E	ALA120
E	CYS121
E	LYS122
E	SER123
E	HIS125
E	GLU126
E	LYS127
E	TYR128
E	ARG129
E	HOH333
J	ARG12
J	GLN13
J	TYR16
J	GLY20
J	TYR58
J	THR71
J	ARG72

site_id	AC5
Number of Residues	18
Details	binding site for Di-peptide HEM E 201 and CYS E 121

Chain	Residue
E	PHE91
E	VAL117
E	GLY118
E	ALA119
E	ALA120
E	LYS122
E	SER123
E	CYS124
E	HIS125
E	ARG129
E	HOH333
J	ARG12
J	GLN13
J	TYR16
J	GLY20
J	TYR58
J	THR71
J	ARG72

site_id	AC6
Number of Residues	17
Details	binding site for Di-peptide HEM F 201 and CYS F 121

Chain	Residue
F	HOH303
F	ARG12
F	GLN13
F	TYR16
F	TYR58
F	THR71
F	ARG72
F	PHE91
F	VAL117
F	GLY118
F	ALA119
F	ALA120
F	LYS122
F	SER123
F	CYS124
F	HIS125
F	ARG129

site_id	AC7
Number of Residues	17
Details	binding site for Di-peptide HEM F 201 and CYS F 124

Chain	Residue
F	ARG12
F	GLN13
F	TYR16
F	TYR58
F	THR71
F	ARG72
F	PHE91
F	ALA120
F	CYS121
F	LYS122
F	SER123
F	HIS125
F	GLU126
F	LYS127
F	TYR128
F	ARG129
F	HOH303

site_id	AC8
Number of Residues	21
Details	binding site for Di-peptide HEM I 201 and CYS I 124

Chain	Residue
I	ARG12
I	GLN13
I	TYR16
I	GLY20
I	TYR58
I	THR71
I	ARG72
I	PHE91
I	ALA120
I	CYS121
I	LYS122
I	SER123
I	HIS125
I	GLU126
I	LYS127
I	TYR128
I	ARG129
I	HOH305
I	HOH313
I	HOH322
N	HOH325

site_id	AC9
Number of Residues	21
Details	binding site for Di-peptide HEM I 201 and CYS I 121

Chain	Residue
I	ARG12
I	GLN13
I	TYR16
I	GLY20
I	TYR58
I	THR71
I	ARG72
I	PHE91
I	VAL117
I	GLY118
I	ALA119
I	ALA120
I	LYS122
I	SER123
I	CYS124
I	HIS125
I	ARG129
I	HOH305
I	HOH313
I	HOH322
N	HOH325

site_id	AD1
Number of Residues	20
Details	binding site for Di-peptide HEM J 201 and CYS J 121

Chain	Residue
E	ARG12
E	GLN13
E	TYR16
E	GLY20
E	TYR58
E	THR71
E	ARG72
J	PHE91
J	VAL117
J	GLY118
J	ALA119
J	ALA120
J	LYS122
J	SER123
J	CYS124
J	HIS125
J	ARG129
J	HOH310
J	HOH314
J	HOH335

site_id	AD2
Number of Residues	20
Details	binding site for Di-peptide HEM J 201 and CYS J 124

Chain	Residue
E	ARG12
E	GLN13
E	TYR16
E	GLY20
E	TYR58
E	THR71
E	ARG72
J	PHE91
J	ALA120
J	CYS121
J	LYS122
J	SER123
J	HIS125
J	GLU126
J	LYS127
J	TYR128
J	ARG129
J	HOH310
J	HOH314
J	HOH335

site_id	AD3
Number of Residues	18
Details	binding site for Di-peptide HEM M 201 and CYS M 121

Chain	Residue
M	ARG12
M	GLN13
M	TYR16
M	TYR58
M	THR71
M	ARG72
M	PHE91
M	VAL117
M	GLY118
M	ALA119
M	ALA120
M	LYS122
M	SER123
M	CYS124
M	HIS125
M	ARG129
M	HOH304
M	HOH309

site_id	AD4
Number of Residues	18
Details	binding site for Di-peptide HEM M 201 and CYS M 124

Chain	Residue
M	ARG12
M	GLN13
M	TYR16
M	TYR58
M	THR71
M	ARG72
M	PHE91
M	ALA120
M	CYS121
M	LYS122
M	SER123
M	HIS125
M	GLU126
M	LYS127
M	TYR128
M	ARG129
M	HOH304
M	HOH309

site_id	AD5
Number of Residues	19
Details	binding site for Di-peptide HEM N 201 and CYS N 121

Chain	Residue
A	ARG12
A	GLN13
A	TYR16
A	TYR58
A	THR71
A	ARG72
N	PHE91
N	VAL117
N	GLY118
N	ALA119
N	ALA120
N	LYS122
N	SER123
N	CYS124
N	HIS125
N	ARG129
N	HOH305
N	HOH317
N	HOH324

site_id	AD6
Number of Residues	19
Details	binding site for Di-peptide HEM N 201 and CYS N 124

Chain	Residue
A	ARG12
A	GLN13
A	TYR16
A	TYR58
A	THR71
A	ARG72
N	PHE91
N	ALA120
N	CYS121
N	LYS122
N	SER123
N	HIS125
N	GLU126
N	LYS127
N	TYR128
N	ARG129
N	HOH305
N	HOH317
N	HOH324

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	BINDING: BINDING => ECO:0000269\|PubMed:8230224, ECO:0007744\|PDB:1BBH

Chain	Residue	Details
J	GLN13
J	ARG72
M	ARG12
M	GLN13
M	ARG72
N	ARG12
N	GLN13
N	ARG72
F	ARG12
F	GLN13
F	ARG72
I	ARG12
I	GLN13
I	ARG72
J	ARG12
E	ARG72
A	ARG12
A	GLN13
A	ARG72
B	ARG12
B	GLN13
B	ARG72
E	ARG12
E	GLN13

site_id	SWS_FT_FI2
Number of Residues	16
Details	BINDING: covalent => ECO:0000269\|PubMed:8230224, ECO:0007744\|PDB:1BBH

Chain	Residue	Details
I	CYS121
I	CYS124
J	CYS121
J	CYS124
M	CYS121
M	CYS124
N	CYS121
N	CYS124
F	CYS124
A	CYS121
A	CYS124
B	CYS121
B	CYS124
E	CYS121
E	CYS124
F	CYS121

site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING: axial binding residue => ECO:0000269\|PubMed:8230224, ECO:0007744\|PDB:1BBH

Chain	Residue	Details
A	HIS125
B	HIS125
E	HIS125
F	HIS125
I	HIS125
J	HIS125
M	HIS125
N	HIS125

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