3SKP

The structure of apo-human transferrin C-lobe with bound sulfate ions

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005576	cellular_component	extracellular region

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 1

Chain	Residue
A	HOH45
A	HOH299
A	HOH327
A	ARG456
A	THR457

---

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 A 680

Chain	Residue
A	HIS350
A	ARG475
A	THR626
A	HOH39
A	HOH111
A	HOH155
A	SER348

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 681

Chain	Residue
A	HOH217
A	HOH306
A	HIS349
A	ARG352
A	SER370
A	HIS473

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 682

Chain	Residue
A	LYS365
A	PRO422
A	HIS642
A	ASP643
A	ARG644

---

site_id	AC5
Number of Residues	11
Details	BINDING SITE FOR RESIDUE SO4 A 683

Chain	Residue
A	HOH18
A	HOH20
A	HOH53
A	HOH296
A	HIS578
A	ALA580
A	ARG581
A	GLY652
A	GLU653
A	GLU654
A	TYR655

---

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 684

Chain	Residue
A	HOH147
A	HOH253
A	HOH325
A	GLN536
A	GLN540
A	ASN618

---

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 685

Chain	Residue
A	HOH162
A	GLY516
A	TYR517
A	THR518
A	HOH690
A	HOH715

---

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 686

Chain	Residue
A	HOH96
A	ALA595
A	HIS598
A	LYS640

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	TYR426-SER435

---

site_id	PS00206
Number of Residues	16
Details	TRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YtGAFRCLvek.GDVAF

Chain	Residue	Details
A	TYR517-PHE532

---

site_id	PS00207
Number of Residues	31
Details	TRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. DYeLLClDgtrkp...VeeyanChlArapnHaVV

Chain	Residue	Details
A	ASP558-VAL588

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
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	ASP392
A	TYR426
A	TYR517
A	HIS585

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00741

Chain	Residue	Details
A	ALA458
A	GLY459
A	THR452
A	ARG456

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039

Chain	Residue	Details
A	SER370
A	SER666

---

site_id	SWS_FT_FI4
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	ASN413

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine; atypical; partial => ECO:0000269|PubMed:15536627

Chain	Residue	Details
A	ASN472

---

site_id	SWS_FT_FI6
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	ASN611

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