2XVY

Cobalt chelatase CbiK (periplasmic) from Desulvobrio vulgaris Hildenborough (co-crystallised with cobalt and SHC)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0016829	molecular_function	lyase activity
A	0016852	molecular_function	sirohydrochlorin cobaltochelatase activity
A	0019251	biological_process	anaerobic cobalamin biosynthetic process
A	0020037	molecular_function	heme binding
A	0042597	cellular_component	periplasmic space
A	0046872	molecular_function	metal ion binding
A	0050897	molecular_function	cobalt ion binding
A	0051262	biological_process	protein tetramerization
A	0051266	molecular_function	sirohydrochlorin ferrochelatase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	BINDING SITE FOR RESIDUE HEM A 1270

Chain	Residue
A	PRO91
A	PRO159
A	HOH2079
A	HOH2217
A	HOH2219
A	HOH2220
A	PRO91
A	GLU93
A	HIS96
A	HIS96
A	LEU99
A	LEU99
A	GLU100
A	LEU119

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CO A 1271

Chain	Residue
A	HIS154
A	GLU184
A	HIS216
A	PER1285
A	HOH2221
A	HOH2222

---

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 A 1272

Chain	Residue
A	HIS88
A	THR89
A	MET210
A	ALA211
A	NA1286
A	HOH2005
A	HOH2223
A	HOH2224
A	HOH2225

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 1273

Chain	Residue
A	GLY92
A	GLU93
A	GLU94
A	THR156
A	HOH2122
A	HOH2226

---

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 1274

Chain	Residue
A	HIS103
A	ARG114
A	VAL115
A	SER116
A	VAL117
A	ARG267

---

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 1275

Chain	Residue
A	PRO140
A	ALA141
A	HOH2112
A	HOH2227

---

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 1276

Chain	Residue
A	LYS144
A	ARG203
A	HOH2229

---

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 1277

Chain	Residue
A	PRO43
A	ARG45
A	HOH2230
A	HOH2231
A	HOH2232

---

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 1278

Chain	Residue
A	GLU249
A	SER250
A	ASP251
A	ALA252

---

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL A 1279

Chain	Residue
A	THR49
A	LYS51
A	MET52

---

site_id	BC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL A 1280

Chain	Residue
A	PRO176
A	ARG199

---

site_id	BC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 1281

Chain	Residue
A	VAL136
A	ARG143
A	ASP175
A	ASP197
A	ARG236
A	HOH2235
A	HOH2236

---

site_id	BC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 1282

Chain	Residue
A	THR19
A	SER20
A	VAL21
A	ILE53
A	GLY214
A	ASP215
A	NA1287

---

site_id	BC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 1283

Chain	Residue
A	GLN8
A	LYS9
A	THR10
A	ASP41
A	PRO43
A	HOH2237

---

site_id	BC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A 1284

Chain	Residue
A	LEU174
A	ASP197
A	VAL198
A	LYS200
A	HOH2238

---

site_id	BC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PER A 1285

Chain	Residue
A	GLU184
A	HIS216
A	CO1271
A	HOH2221
A	HOH2222

---

site_id	BC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA A 1286

Chain	Residue
A	THR89
A	GLY153
A	HIS154
A	TYR164
A	LEU209
A	SO41272

---

site_id	BC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE NA A 1287

Chain	Residue
A	HIS216
A	GOL1282
A	ASP215

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000305|PubMed:21173279

Chain	Residue	Details
A	HIS154

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: axial binding residue => ECO:0000269|PubMed:21173279, ECO:0007744|PDB:2XVX, ECO:0007744|PDB:2XVZ

Chain	Residue	Details
A	HIS96

---

site_id	SWS_FT_FI3
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:21173279, ECO:0007744|PDB:2XVZ

Chain	Residue	Details
A	HIS154
A	GLU184
A	HIS216

---