Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2O7U

Crystal structure of K206E/K296E mutant of the N-terminal half molecule of human transferrin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005576	cellular_component	extracellular region
B	0005576	cellular_component	extracellular region
C	0005576	cellular_component	extracellular region
D	0005576	cellular_component	extracellular region
E	0005576	cellular_component	extracellular region
F	0005576	cellular_component	extracellular region
G	0005576	cellular_component	extracellular region
H	0005576	cellular_component	extracellular region
I	0005576	cellular_component	extracellular region

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE B 500

Chain	Residue
B	ASP63
B	TYR95
B	TYR188
B	HIS249
B	CO3600

site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE CO3 B 600

Chain	Residue
B	ALA126
B	GLY127
B	TYR188
B	HIS249
B	FE500
B	ASP63
B	TYR95
B	THR120
B	ARG124

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE A 500

Chain	Residue
A	ASP63
A	TYR95
A	TYR188
A	HIS249
A	CO3600

site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE CO3 A 600

Chain	Residue
A	ASP63
A	TYR95
A	THR120
A	ARG124
A	ALA126
A	GLY127
A	TYR188
A	HIS249
A	FE500

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE C 500

Chain	Residue
C	ASP63
C	TYR95
C	TYR188
C	HIS249
C	CO3600

site_id	AC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE CO3 C 600

Chain	Residue
C	ASP63
C	TYR95
C	THR120
C	ARG124
C	ALA126
C	GLY127
C	TYR188
C	HIS249
C	FE500

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE D 500

Chain	Residue
D	ASP63
D	TYR95
D	TYR188
D	HIS249
D	CO3600

site_id	AC8
Number of Residues	10
Details	BINDING SITE FOR RESIDUE CO3 D 600

Chain	Residue
D	ASP63
D	TYR95
D	THR120
D	ARG124
D	SER125
D	ALA126
D	GLY127
D	TYR188
D	HIS249
D	FE500

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE E 500

Chain	Residue
E	ASP63
E	TYR95
E	TYR188
E	HIS249
E	CO3600

site_id	BC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE CO3 E 600

Chain	Residue
E	ASP63
E	TYR95
E	THR120
E	ARG124
E	SER125
E	ALA126
E	GLY127
E	TYR188
E	HIS249
E	FE500

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE F 500

Chain	Residue
F	ASP63
F	TYR95
F	TYR188
F	HIS249
F	CO3600

site_id	BC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE CO3 F 600

Chain	Residue
F	ASP63
F	TYR95
F	THR120
F	ARG124
F	SER125
F	ALA126
F	GLY127
F	TYR188
F	HIS249
F	FE500

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE G 500

Chain	Residue
G	ASP63
G	TYR95
G	TYR188
G	HIS249
G	CO3600

site_id	BC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE CO3 G 600

Chain	Residue
G	TYR188
G	FE500
G	ASP63
G	TYR95
G	THR120
G	ARG124
G	SER125
G	ALA126
G	GLY127

site_id	BC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE H 500

Chain	Residue
H	ASP63
H	TYR95
H	TYR188
H	HIS249
H	CO3600

site_id	BC7
Number of Residues	10
Details	BINDING SITE FOR RESIDUE CO3 H 600

Chain	Residue
H	ASP63
H	TYR95
H	THR120
H	ARG124
H	SER125
H	ALA126
H	GLY127
H	TYR188
H	HIS249
H	FE500

site_id	BC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE I 500

Chain	Residue
I	ASP63
I	TYR95
I	TYR188
I	HIS249
I	CO3600

site_id	BC9
Number of Residues	9
Details	BINDING SITE FOR RESIDUE CO3 I 600

Chain	Residue
I	ASP63
I	TYR95
I	THR120
I	ARG124
I	SER125
I	ALA126
I	GLY127
I	TYR188
I	FE500

Functional Information from PROSITE/UniProt

site_id	PS00205
Number of Residues	10
Details	TRANSFERRIN_LIKE_1 Transferrin-like domain signature 1. YyAVAVVKKD

Chain	Residue	Details
B	TYR95-ASP104

site_id	PS00206
Number of Residues	17
Details	TRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YsGAFKCLkdgaGDVAF

Chain	Residue	Details
B	TYR188-PHE204

site_id	PS00207
Number of Residues	31
Details	TRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. QYeLLClDntrkp...VdeykdChlAqvpsHtVV

Chain	Residue	Details
B	GLN222-VAL252

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	36
Details	BINDING: BINDING => ECO:0000269\|PubMed:22327295, ECO:0007744\|PDB:3V83

Chain	Residue	Details
B	ASP63
B	TYR95
B	TYR188
B	HIS249
A	ASP63
A	TYR95
A	TYR188
A	HIS249
C	ASP63
C	TYR95
C	TYR188
C	HIS249
D	ASP63
D	TYR95
D	TYR188
D	HIS249
E	ASP63
E	TYR95
E	TYR188
E	HIS249
F	ASP63
F	TYR95
F	TYR188
F	HIS249
G	ASP63
G	TYR95
G	TYR188
G	HIS249
H	ASP63
H	TYR95
H	TYR188
H	HIS249
I	ASP63
I	TYR95
I	TYR188
I	HIS249

site_id	SWS_FT_FI2
Number of Residues	36
Details	BINDING:

Chain	Residue	Details
B	THR120
B	ARG124
E	ALA126
E	GLY127
F	THR120
F	ARG124
F	ALA126
F	GLY127
G	THR120
G	ARG124
G	ALA126
G	GLY127
H	THR120
H	ARG124
H	ALA126
H	GLY127
I	THR120
I	ARG124
I	ALA126
I	GLY127
B	ALA126
B	GLY127
A	THR120
A	ARG124
A	ALA126
A	GLY127
C	THR120
C	ARG124
C	ALA126
C	GLY127
D	THR120
D	ARG124
D	ALA126
D	GLY127
E	THR120
E	ARG124

site_id	SWS_FT_FI3
Number of Residues	9
Details	MOD_RES: Dimethylated arginine => ECO:0000250\|UniProtKB:P12346

Chain	Residue	Details
B	ARG23
A	ARG23
C	ARG23
D	ARG23
E	ARG23
F	ARG23
G	ARG23
H	ARG23
I	ARG23

site_id	SWS_FT_FI4
Number of Residues	9
Details	CARBOHYD: O-linked (GalNAc...) serine

Chain	Residue	Details
H	SER32
B	SER32
A	SER32
C	SER32
D	SER32
E	SER32
F	SER32
G	SER32
I	SER32

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