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4XC7

Isobutyryl-CoA mutase fused with bound butyryl-CoA and without cobalamin or GDP (apo-IcmF)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0003824molecular_functioncatalytic activity
A0003924molecular_functionGTPase activity
A0004494molecular_functionmethylmalonyl-CoA mutase activity
A0005525molecular_functionGTP binding
A0006637biological_processacyl-CoA metabolic process
A0008152biological_processmetabolic process
A0016787molecular_functionhydrolase activity
A0016853molecular_functionisomerase activity
A0016866molecular_functionintramolecular transferase activity
A0031419molecular_functioncobalamin binding
A0034784molecular_functionpivalyl-CoA mutase activity
A0046872molecular_functionmetal ion binding
A0047727molecular_functionisobutyryl-CoA mutase activity
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0003824molecular_functioncatalytic activity
B0003924molecular_functionGTPase activity
B0004494molecular_functionmethylmalonyl-CoA mutase activity
B0005525molecular_functionGTP binding
B0006637biological_processacyl-CoA metabolic process
B0008152biological_processmetabolic process
B0016787molecular_functionhydrolase activity
B0016853molecular_functionisomerase activity
B0016866molecular_functionintramolecular transferase activity
B0031419molecular_functioncobalamin binding
B0034784molecular_functionpivalyl-CoA mutase activity
B0046872molecular_functionmetal ion binding
B0047727molecular_functionisobutyryl-CoA mutase activity
Functional Information from PDB Data
site_idAC1
Number of Residues20
Detailsbinding site for residue BCO A 1101
ChainResidue
APHE585
AARG728
ATHR730
AGLN732
ATYR772
ASER821
APHE823
AARG856
ALYS861
AHIS863
AGLN865
APHE587
ASER897
AARG589
AARG596
APHE598
AARG622
ASER624
ASER677
ATHR679

site_idAC2
Number of Residues6
Detailsbinding site for residue TLA A 1102
ChainResidue
AGLY219
AGLY221
ASER223
ASER224
AARG265
ALYS358

site_idAC3
Number of Residues3
Detailsbinding site for residue BCO B 1101
ChainResidue
BPHE585
BPHE587
BARG728

site_idAC4
Number of Residues10
Detailsbinding site for residue TLA B 1102
ChainResidue
BGLY219
BGLY221
BLYS222
BSER223
BSER224
BARG265
BGLY337
BALA338
BGLN341
BLYS358

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: axial binding residue => ECO:0000255|HAMAP-Rule:MF_02050, ECO:0000269|PubMed:25675500, ECO:0007744|PDB:4XC6
ChainResidueDetails
AHIS39
BHIS39

site_idSWS_FT_FI2
Number of Residues22
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02050, ECO:0000269|PubMed:25675500, ECO:0007744|PDB:4XC6
ChainResidueDetails
AGLY219
AGLU973
AASN1092
BGLY219
BSER223
BILE248
BASP249
BASP262
BARG265
BGLU310
BTHR311
ASER223
BASN357
BGLU973
BASN1092
AILE248
AASP249
AASP262
AARG265
AGLU310
ATHR311
AASN357

site_idSWS_FT_FI3
Number of Residues14
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02050, ECO:0000269|PubMed:25675500
ChainResidueDetails
APHE587
BARG728
BTYR772
BSER821
BARG856
BLYS861
AARG622
AARG728
ATYR772
ASER821
AARG856
ALYS861
BPHE587
BARG622

218853

PDB entries from 2024-04-24

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