5DYH

Ti(IV) bound human serum transferrin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0006826	biological_process	iron ion transport
A	0006879	biological_process	intracellular iron ion homeostasis
A	0008199	molecular_function	ferric iron binding
B	0005576	cellular_component	extracellular region
B	0005615	cellular_component	extracellular space
B	0006826	biological_process	iron ion transport
B	0006879	biological_process	intracellular iron ion homeostasis
B	0008199	molecular_function	ferric iron binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue CIT A 701

Chain	Residue
A	TYR426
A	ARG456
A	THR457
A	TYR517
A	4TI707
A	CO3708

---

site_id	AC2
Number of Residues	5
Details	binding site for residue CIT A 702

Chain	Residue
A	TYR188
A	LYS206
A	TYR95
A	ARG124
A	SER125

---

site_id	AC3
Number of Residues	4
Details	binding site for residue CIT A 703

Chain	Residue
A	ARG456
A	GLY516
A	TYR517
A	THR518

---

site_id	AC4
Number of Residues	4
Details	binding site for residue CIT A 704

Chain	Residue
A	ARG124
A	GLY187
A	TYR188
A	SER189

---

site_id	AC5
Number of Residues	4
Details	binding site for residue CIT A 705

Chain	Residue
A	GLU338
A	LYS599
B	ARG602
B	HIS606

---

site_id	AC6
Number of Residues	3
Details	binding site for residue CIT A 706

Chain	Residue
A	HIS578
A	ARG581
A	GLU654

---

site_id	AC7
Number of Residues	4
Details	binding site for residue 4TI A 707

Chain	Residue
A	TYR426
A	TYR517
A	CIT701
A	CO3708

---

site_id	AC8
Number of Residues	9
Details	binding site for residue CO3 A 708

Chain	Residue
A	TYR426
A	THR452
A	ARG456
A	THR457
A	ALA458
A	GLY459
A	TYR517
A	CIT701
A	4TI707

---

site_id	AC9
Number of Residues	7
Details	binding site for residue CIT B 701

Chain	Residue
B	TYR426
B	ARG456
B	THR457
B	TYR517
B	CIT702
B	4TI706
B	CO3707

---

site_id	AD1
Number of Residues	6
Details	binding site for residue CIT B 702

Chain	Residue
B	ARG456
B	TYR515
B	GLY516
B	TYR517
B	THR518
B	CIT701

---

site_id	AD2
Number of Residues	5
Details	binding site for residue CIT B 703

Chain	Residue
B	TYR95
B	ARG124
B	SER125
B	TYR188
B	LYS206

---

site_id	AD3
Number of Residues	5
Details	binding site for residue CIT B 704

Chain	Residue
B	ARG124
B	PHE186
B	GLY187
B	TYR188
B	SER189

---

site_id	AD4
Number of Residues	6
Details	binding site for residue CIT B 705

Chain	Residue
A	SER348
A	HIS349
A	HIS350
B	SER348
B	HIS349
B	HIS350

---

site_id	AD5
Number of Residues	4
Details	binding site for residue 4TI B 706

Chain	Residue
B	TYR426
B	TYR517
B	CIT701
B	CO3707

---

site_id	AD6
Number of Residues	9
Details	binding site for residue CO3 B 707

Chain	Residue
B	TYR426
B	THR452
B	ARG456
B	THR457
B	ALA458
B	GLY459
B	TYR517
B	CIT701
B	4TI706

---

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
A	TYR95-ASP104

---

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

Chain	Residue	Details
A	TYR188-PHE204
A	TYR517-PHE532

---

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

Chain	Residue	Details
A	GLN222-VAL252
A	ASP558-VAL588

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|PubMed:22327295, ECO:0007744|PDB:3V83

Chain	Residue	Details
A	ASP63
A	TYR95
A	TYR188
A	HIS249
B	ASP63
B	TYR95
B	TYR188
B	HIS249

---

site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING:

Chain	Residue	Details
A	THR120
A	ARG124
A	ALA126
A	GLY127
B	THR120
B	ARG124
B	ALA126
B	GLY127

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:22327295, ECO:0000269|PubMed:22343719, ECO:0000269|PubMed:31636418, ECO:0007744|PDB:3V83, ECO:0007744|PDB:3VE1, ECO:0007744|PDB:6SOY, ECO:0007744|PDB:6SOZ

Chain	Residue	Details
A	ASP392
A	TYR426
A	TYR517
A	HIS585
B	ASP392
B	TYR426
B	TYR517
B	HIS585

---

site_id	SWS_FT_FI4
Number of Residues	8
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00741

Chain	Residue	Details
A	THR452
A	ARG456
A	ALA458
A	GLY459
B	THR452
B	ARG456
B	ALA458
B	GLY459

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Dimethylated arginine => ECO:0000250|UniProtKB:P12346

Chain	Residue	Details
A	ARG23
B	ARG23

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	MOD_RES: Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039

Chain	Residue	Details
A	SER370
A	SER666
B	SER370
B	SER666

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	CARBOHYD: O-linked (GalNAc...) serine

Chain	Residue	Details
A	SER32
B	SER32

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:15536627, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:22327295, ECO:0000269|PubMed:31636418, ECO:0007744|PDB:6SOY, ECO:0007744|PDB:6SOZ

Chain	Residue	Details
A	ASN413
B	ASN413

---

site_id	SWS_FT_FI9
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine; atypical; partial => ECO:0000269|PubMed:15536627

Chain	Residue	Details
A	ASN472
B	ASN472

---

site_id	SWS_FT_FI10
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:15536627, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:22327295

Chain	Residue	Details
A	ASN611
B	ASN611

---