6UJ6

X-ray Crystal Structure of Chromium-transferrin with Synergistic Anion Malonate

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue CR A 701

Chain	Residue
A	ASP411
A	TYR445
A	TYR536
A	HIS604
A	MLI702

---

site_id	AC2
Number of Residues	10
Details	binding site for residue MLI A 702

Chain	Residue
A	THR476
A	ALA477
A	GLY478
A	TYR536
A	HIS604
A	CR701
A	ASP411
A	TYR445
A	THR471
A	ARG475

---

site_id	AC3
Number of Residues	6
Details	binding site for residue GOL A 703

Chain	Residue
A	CYS246
A	LEU247
A	ASP248
A	ASP259
A	CYS260
A	HIS261

---

site_id	AC4
Number of Residues	2
Details	binding site for residue GOL A 704

Chain	Residue
A	MET128
A	ASP157

---

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

Chain	Residue
A	GLU429
A	HIS604
A	LEU649
A	ARG651

---

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	TYR114-ASP123
A	TYR445-SER454

---

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

Chain	Residue	Details
A	TYR207-PHE223
A	TYR536-PHE551

---

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

Chain	Residue	Details
A	GLN241-VAL271
A	ASP577-VAL607

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:22327295, ECO:0007744|PDB:3V83

Chain	Residue	Details
A	ASP82
A	TYR114
A	TYR207
A	HIS268

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING:

Chain	Residue	Details
A	THR139
A	ARG143
A	ALA145
A	GLY146

---

site_id	SWS_FT_FI3
Number of Residues	4
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	ASP411
A	TYR445
A	TYR536
A	HIS604

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00741

Chain	Residue	Details
A	THR471
A	ARG475
A	ALA477
A	GLY478

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Dimethylated arginine => ECO:0000250|UniProtKB:P12346

Chain	Residue	Details
A	ARG42

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039

Chain	Residue	Details
A	SER389
A	SER685

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	CARBOHYD: O-linked (GalNAc...) serine

Chain	Residue	Details
A	SER51

---

site_id	SWS_FT_FI8
Number of Residues	1
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	ASN432

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine; atypical; partial => ECO:0000269|PubMed:15536627

Chain	Residue	Details
A	ASN491

---

site_id	SWS_FT_FI10
Number of Residues	1
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	ASN630

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