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2XVX

Cobalt chelatase CbiK (periplasmatic) from Desulvobrio vulgaris Hildenborough (Native)

Functional Information from GO Data
ChainGOidnamespacecontents
A0016829molecular_functionlyase activity
A0016852molecular_functionsirohydrochlorin cobaltochelatase activity
A0019251biological_processanaerobic cobalamin biosynthetic process
A0020037molecular_functionheme binding
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
A0050897molecular_functioncobalt ion binding
A0051262biological_processprotein tetramerization
A0051266molecular_functionsirohydrochlorin ferrochelatase activity
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE HEM A 1270
ChainResidue
APRO91
ALEU119
AHIS158
APRO159
AHOH2070
AHOH2200
APRO91
AGLU93
AHIS96
AHIS96
ALEU99
ALEU99
AGLU100
AHIS103

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 1271
ChainResidue
AGLY92
AGLU93
AGLU94
ATHR156
AHIS158
AHOH2069

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 1272
ChainResidue
AHIS103
AARG114
AVAL115
ASER116
AVAL117
AARG267

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 1273
ChainResidue
ALEU87
AHIS88
ATHR89
AHIS154
AMET210
AALA211
ANA1288
AHOH2202
AHOH2203

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 1274
ChainResidue
APRO43
AVAL44
AARG45
AHOH2204

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 1275
ChainResidue
ATHR19
ASER20
AVAL21
AILE53
AGLY214
AASP215
AGOL1284

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 1276
ChainResidue
AVAL136
AARG143
AASP175
AASP197
AARG236
AHOH2206

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 1277
ChainResidue
ATHR49
ALYS51
AMET52

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 1278
ChainResidue
ALYS144
AARG203
AGOL1279
AHOH2111

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 1279
ChainResidue
ALYS144
AARG203
AGLU239
AGOL1278
AHOH2209

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 1280
ChainResidue
AGOL1285
AHOH2210
AHOH2211
AHOH2212

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 1281
ChainResidue
APRO176
AASP197
AVAL198
AHOH2206
AHOH2213

site_idBC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 1282
ChainResidue
ASER250
AASP251
AALA252

site_idBC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL A 1283
ChainResidue
APRO176
AARG199

site_idBC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 1284
ChainResidue
APHE17
AHIS154
AGLY214
AASP215
AHIS216
ASO41275

site_idBC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 1285
ChainResidue
AARG58
AARG58
AILE62
AGOL1280
AHOH2214
AHOH2214
AHOH2215

site_idBC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CO2 A 1286
ChainResidue
AGLU184
AHIS216
AHOH2217

site_idBC9
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 1287
ChainResidue
AALA141

site_idCC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 1288
ChainResidue
ASO41273
ATHR89
AGLY153
AHIS154
ATYR164

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"21173279","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"21173279","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2XVX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XVZ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21173279","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2XVZ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

245663

PDB entries from 2025-12-03

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