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2XVZ

Cobalt chelatase CbiK (periplasmatic) from Desulvobrio vulgaris Hildenborough (co-crystallized with cobalt)

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 Residues9
DetailsBINDING SITE FOR RESIDUE HEM A 1270
ChainResidue
APRO91
AHIS96
AHIS96
ALEU99
ALEU99
ALEU119
APRO159
AHOH2040
AHOH2105

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO A 1271
ChainResidue
AHIS154
AGLU184
AHIS216
APER1285
AHOH2106

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 1272
ChainResidue
AGLY92
AGLU93
AGLU94
ATHR156
AHIS158
AHOH2037
AHOH2055
AHOH2107

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 1273
ChainResidue
APHE17
ALEU87
AHIS88
ATHR89
AMET210
AALA211
ANA1283
AHOH2108

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 1274
ChainResidue
AARG114
AVAL115
ASER116
AVAL117
AARG267

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 1275
ChainResidue
ALEU174
AASP175
AASP197
AARG236
AHOH2065

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 1276
ChainResidue
ATRP172
APRO176
AARG199

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 1277
ChainResidue
ATHR49
ALYS51
AMET52
AGLU94

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 1278
ChainResidue
APRO140
AALA141
AHOH2109

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 1279
ChainResidue
ASER250
AASP251
AALA252

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 1280
ChainResidue
ATHR19
ASER20
AVAL21
AASP215
ASO41281
AHOH2110

site_idBC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 1281
ChainResidue
AGLY214
AASP215
AHIS216
ASO41280
AHOH2106
AHOH2110
AHOH2111

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 1282
ChainResidue
APRO43
AVAL44
AARG45
AHOH2112

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 1283
ChainResidue
AGLY153
AHIS154
ATYR164
ASO41273

site_idBC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PER A 1285
ChainResidue
AHIS154
AGLU184
AHIS216
ACO1271

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:21173279
ChainResidueDetails
AHIS154

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:21173279, ECO:0007744|PDB:2XVX, ECO:0007744|PDB:2XVZ
ChainResidueDetails
AHIS96

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:21173279, ECO:0007744|PDB:2XVZ
ChainResidueDetails
AHIS154
AGLU184
AHIS216

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PDB entries from 2024-08-14

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