2BB6

Structure of Cobalamin-complexed Bovine Transcobalamin in Monoclinic Crystal Form

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0006824	biological_process	cobalt ion transport
A	0015889	biological_process	cobalamin transport
A	0031419	molecular_function	cobalamin binding
A	0046872	molecular_function	metal ion binding
B	0005576	cellular_component	extracellular region
B	0005615	cellular_component	extracellular space
B	0006824	biological_process	cobalt ion transport
B	0015889	biological_process	cobalamin transport
B	0031419	molecular_function	cobalamin binding
B	0046872	molecular_function	metal ion binding
C	0005576	cellular_component	extracellular region
C	0005615	cellular_component	extracellular space
C	0006824	biological_process	cobalt ion transport
C	0015889	biological_process	cobalamin transport
C	0031419	molecular_function	cobalamin binding
C	0046872	molecular_function	metal ion binding
D	0005576	cellular_component	extracellular region
D	0005615	cellular_component	extracellular space
D	0006824	biological_process	cobalt ion transport
D	0015889	biological_process	cobalamin transport
D	0031419	molecular_function	cobalamin binding
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CL A 901

Chain	Residue
A	B120
A	TYR229
A	THR267
A	GLN269
A	ASN270
A	GLN394

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CL B 902

Chain	Residue
B	GLN269
B	ASN270
B	GLN394
B	B120
B	TYR229
B	THR267

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CL C 904

Chain	Residue
C	B120
C	TYR229
C	THR267
C	GLN269
C	ASN270
C	GLN394

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CL D 903

Chain	Residue
D	B120
D	TYR229
D	THR267
D	GLN269
D	ASN270
D	GLN394

---

site_id	AC5
Number of Residues	39
Details	BINDING SITE FOR RESIDUE B12 A 0

Chain	Residue
A	GLY85
A	GLN86
A	THR134
A	TYR137
A	GLN138
A	HIS175
A	VAL176
A	ASP179
A	ASN227
A	TYR229
A	SER230
A	ASN270
A	MET273
A	GLN276
A	SER362
A	LEU363
A	SER364
A	GLY365
A	PRO366
A	PHE367
A	LEU368
A	PHE381
A	TRP382
A	GLN383
A	VAL384
A	LEU392
A	GLN393
A	GLY395
A	TRP414
A	CL901
A	HOH904
A	HOH905
A	HOH906
A	HOH913
A	HOH917
A	HOH918
A	HOH991
A	HOH1038
A	HOH1051

---

site_id	AC6
Number of Residues	40
Details	BINDING SITE FOR RESIDUE B12 B 0

Chain	Residue
B	HOH921
B	HOH988
B	HOH1002
B	HOH1083
B	GLY85
B	GLN86
B	THR134
B	TYR137
B	GLN138
B	HIS175
B	VAL176
B	ASP179
B	ASN227
B	TYR229
B	SER230
B	ASN270
B	MET273
B	GLN276
B	SER362
B	LEU363
B	SER364
B	GLY365
B	PRO366
B	PHE367
B	LEU368
B	PHE381
B	TRP382
B	GLN383
B	VAL384
B	LEU392
B	GLN393
B	GLN394
B	GLY395
B	TRP414
B	CL902
B	HOH904
B	HOH906
B	HOH910
B	HOH912
B	HOH913

---

site_id	AC7
Number of Residues	39
Details	BINDING SITE FOR RESIDUE B12 C 0

Chain	Residue
C	GLY85
C	GLN86
C	THR134
C	TYR137
C	GLN138
C	HIS175
C	ASP179
C	ASN227
C	TYR229
C	SER230
C	LEU233
C	ASN270
C	MET273
C	GLN276
C	SER362
C	LEU363
C	SER364
C	GLY365
C	PRO366
C	PHE367
C	LEU368
C	PHE381
C	TRP382
C	GLN383
C	VAL384
C	LEU392
C	GLN393
C	GLN394
C	GLY395
C	TRP414
C	CL904
C	HOH907
C	HOH909
C	HOH914
C	HOH918
C	HOH930
C	HOH948
C	HOH964
C	HOH986

---

site_id	AC8
Number of Residues	38
Details	BINDING SITE FOR RESIDUE B12 D 0

Chain	Residue
D	GLY85
D	GLN86
D	THR134
D	TYR137
D	GLN138
D	HIS175
D	ASP179
D	ASN227
D	TYR229
D	SER230
D	LEU233
D	ASN270
D	MET273
D	GLN276
D	SER362
D	LEU363
D	SER364
D	GLY365
D	PRO366
D	PHE367
D	LEU368
D	PHE381
D	TRP382
D	GLN383
D	VAL384
D	LEU392
D	GLN393
D	GLY395
D	TRP414
D	CL903
D	HOH904
D	HOH906
D	HOH907
D	HOH912
D	HOH919
D	HOH945
D	HOH964
D	HOH966

---

Functional Information from PROSITE/UniProt

site_id	PS00468
Number of Residues	14
Details	COBALAMIN_BINDING Eukaryotic cobalamin-binding proteins signature. SVDTMAMAgMAFSC

Chain	Residue	Details
A	SER177-CYS190

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	16
Details	BINDING: BINDING => ECO:0000269|PubMed:16537422, ECO:0000269|PubMed:17943552

Chain	Residue	Details
A	GLN86
C	ASN227
C	SER230
C	GLN276
D	GLN86
D	ASN227
D	SER230
D	GLN276
A	ASN227
A	SER230
A	GLN276
B	GLN86
B	ASN227
B	SER230
B	GLN276
C	GLN86

---

site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING:

Chain	Residue	Details
A	THR134
A	TRP382
B	THR134
B	TRP382
C	THR134
C	TRP382
D	THR134
D	TRP382

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: axial binding residue

Chain	Residue	Details
A	HIS175
B	HIS175
C	HIS175
D	HIS175

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	ASN76
B	ASN76
C	ASN76
D	ASN76

---