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1C9K

THE THREE DIMENSIONAL STRUCTURE OF ADENOSYLCOBINAMIDE KINASE/ ADENOSYLCOBINAMIDE PHOSPHATE GUALYLYLTRANSFERASE (COBU) COMPLEXED WITH GMP: EVIDENCE FOR A SUBSTRATE INDUCED TRANSFERASE ACTIVE SITE

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005524molecular_functionATP binding
A0005525molecular_functionGTP binding
A0008820molecular_functioncobinamide phosphate guanylyltransferase activity
A0009236biological_processcobalamin biosynthetic process
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0036428molecular_functionadenosylcobinamide kinase (GTP-specific) activity
A0036429molecular_functionadenosylcobinamide kinase (ATP-specific) activity
A0043752molecular_functionadenosylcobinamide kinase activity
B0000166molecular_functionnucleotide binding
B0005524molecular_functionATP binding
B0005525molecular_functionGTP binding
B0008820molecular_functioncobinamide phosphate guanylyltransferase activity
B0009236biological_processcobalamin biosynthetic process
B0016301molecular_functionkinase activity
B0016310biological_processphosphorylation
B0036428molecular_functionadenosylcobinamide kinase (GTP-specific) activity
B0036429molecular_functionadenosylcobinamide kinase (ATP-specific) activity
B0043752molecular_functionadenosylcobinamide kinase activity
C0000166molecular_functionnucleotide binding
C0005524molecular_functionATP binding
C0005525molecular_functionGTP binding
C0008820molecular_functioncobinamide phosphate guanylyltransferase activity
C0009236biological_processcobalamin biosynthetic process
C0016301molecular_functionkinase activity
C0016310biological_processphosphorylation
C0036428molecular_functionadenosylcobinamide kinase (GTP-specific) activity
C0036429molecular_functionadenosylcobinamide kinase (ATP-specific) activity
C0043752molecular_functionadenosylcobinamide kinase activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 A 600
ChainResidue
AGLY7
AARG9
ASER10
AGLY11
ALYS12
ASER13
AHOH851

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 B 601
ChainResidue
BSER10
BGLY11
BLYS12
BSER13
BHOH725
BHOH749
BGLY7
BARG9

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG C 607
ChainResidue
CSER13
CGLU80
CPOP608

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE 5GP A 604
ChainResidue
ATYR28
AALA30
ATHR31
ASER32
AILE34
AILE43
AHIS46
ALYS47
AARG50
AGLU58
AGLU80
ACYS81

site_idAC5
Number of Residues12
DetailsBINDING SITE FOR RESIDUE 5GP B 605
ChainResidue
BSER13
BTYR28
BALA30
BTHR31
BSER32
BILE43
BHIS46
BLYS47
BARG50
BGLU58
BGLU80
BCYS81

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE POP C 608
ChainResidue
CGLY7
CALA8
CARG9
CSER10
CGLY11
CLYS12
CSER13
CMG607
CHOH739
CHOH898

site_idAC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 5GP C 606
ChainResidue
CTYR28
CALA30
CTHR31
CSER32
CILE34
CLYS47
CARG50
CGLU80
CCYS81
CTHR84

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: GMP-histidine intermediate => ECO:0000269|PubMed:10529169
ChainResidueDetails
AHIS46
BHIS46
CHIS46

site_idSWS_FT_FI2
Number of Residues15
DetailsBINDING:
ChainResidueDetails
AGLY6
BGLU80
CGLY6
CALA30
CLYS47
CGLU58
CGLU80
AALA30
ALYS47
AGLU58
AGLU80
BGLY6
BALA30
BLYS47
BGLU58

224931

PDB entries from 2024-09-11

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