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4KQH

Crystal structure of CobT E317A

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0008939molecular_functionnicotinate-nucleotide-dimethylbenzimidazole phosphoribosyltransferase activity
A0009236biological_processcobalamin biosynthetic process
A0016757molecular_functionglycosyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 701
ChainResidue
AGLY264
APHE265
ALEU266
ASER291
ALEU315
AHOH858
AHOH859
AHOH882
AHOH985

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 702
ChainResidue
AARG38
AARG282
AMET305
AGLU306
AHOH804
AHOH805

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO A 703
ChainResidue
ACYS275
AARG282
ALEU303
AHOH864
AHOH945
AHOH972
AHOH996
AHOH1058

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 A 704
ChainResidue
AALA78
AALA178
AASN179
ATHR180
AHOH901
AHOH938
AHOH939

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305|PubMed:11441022
ChainResidueDetails
AGLN88

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:24121107, ECO:0000269|DOI:10.1074/jbc.M203535200
ChainResidueDetails
AGLU174
AALA203
APHE265
ASER291
AARG314

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Important for substrate positioning, might be proton acceptor => ECO:0000269|PubMed:24121107
ChainResidueDetails
AGLU174

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Important for substrate positioning, might be proton acceptor => ECO:0000269|PubMed:24121107, ECO:0000305|PubMed:10587435, ECO:0000305|DOI:10.1074/jbc.M203535200
ChainResidueDetails
AALA317

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 79
ChainResidueDetails
AGLU174electrostatic stabiliser, unknown
AALA317activator, hydrogen bond acceptor, proton acceptor, unknown

219515

PDB entries from 2024-05-08

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