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4R3U

Crystal structure of 2-Hydroxyisobutyryl-CoA Mutase

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004494molecular_functionmethylmalonyl-CoA mutase activity
A0016853molecular_functionisomerase activity
A0016866molecular_functionintramolecular transferase activity
A0031419molecular_functioncobalamin binding
B0003824molecular_functioncatalytic activity
B0004494molecular_functionmethylmalonyl-CoA mutase activity
B0016853molecular_functionisomerase activity
B0016866molecular_functionintramolecular transferase activity
B0031419molecular_functioncobalamin binding
C0016853molecular_functionisomerase activity
C0031419molecular_functioncobalamin binding
C0046872molecular_functionmetal ion binding
D0016853molecular_functionisomerase activity
D0031419molecular_functioncobalamin binding
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues42
DetailsBINDING SITE FOR RESIDUE 3HC A 801
ChainResidue
APHE27
ASER115
AASP117
ASER165
ATHR167
ATHR196
AGLN198
AGLN208
AARG235
AASN237
AASN240
ATYR76
ATYR244
AHIS245
AARG284
AALA286
APHE288
AARG328
APHE329
AHIS330
AGLN332
AGLN363
ATHR78
ASER364
A5AD803
AHOH911
AHOH917
AHOH939
AHOH945
AHOH977
AHOH999
AHOH1006
AHOH1009
AMET79
AHOH1021
AHOH1054
CB12800
ASER82
AARG83
ATHR86
AARG88
AILE90

site_idAC2
Number of Residues41
DetailsBINDING SITE FOR RESIDUE 3KK A 802
ChainResidue
APHE27
ATYR76
ATHR78
AMET79
ASER82
AARG83
ATHR86
AARG88
AILE90
ASER115
AASP117
ASER165
ATHR167
ATHR196
AGLN198
AGLN208
AARG235
AASN237
AASN240
ATYR244
AHIS245
AARG284
AALA286
APHE288
AARG328
APHE329
AHIS330
AGLN332
AGLN363
ASER364
A5AD803
AHOH911
AHOH917
AHOH939
AHOH945
AHOH977
AHOH999
AHOH1006
AHOH1009
AHOH1021
CB12800

site_idAC3
Number of Residues22
DetailsBINDING SITE FOR RESIDUE 5AD A 803
ChainResidue
AHOH1053
AHOH1054
AHOH1056
AHOH1057
CB12800
CHOH938
AILE90
AGLY92
AASP117
AGLU140
ATYR244
AGLN332
AALA335
AASN368
AGLU372
AILE376
APRO377
A3HC801
A3KK802
AHOH923
AHOH978
AHOH1052

site_idAC4
Number of Residues32
DetailsBINDING SITE FOR RESIDUE 3HC B 801
ChainResidue
BPHE27
BALA31
BTYR76
BTHR78
BMET79
BSER82
BARG83
BTHR86
BARG88
BILE90
BSER115
BASP117
BSER165
BTHR167
BTHR196
BGLN198
BGLN208
BARG235
BASN237
BASN240
BTYR244
BHIS245
BARG284
BALA286
BPHE288
BARG328
BPHE329
BHIS330
BGLN332
BGLN363
BSER364
DB12800

site_idAC5
Number of Residues31
DetailsBINDING SITE FOR RESIDUE 3KK B 802
ChainResidue
BPHE27
BTYR76
BTHR78
BMET79
BSER82
BARG83
BTHR86
BARG88
BILE90
BSER115
BASP117
BSER165
BTHR167
BTHR196
BGLN198
BGLN208
BARG235
BASN237
BASN240
BTYR244
BHIS245
BARG284
BALA286
BPHE288
BARG328
BPHE329
BHIS330
BGLN332
BGLN363
BSER364
DB12800

site_idAC6
Number of Residues47
DetailsBINDING SITE FOR RESIDUE B12 C 800
ChainResidue
AASP117
APHE118
AMET120
ALEU123
AGLU140
AALA207
AGLN208
AGLU210
AGLU248
AALA249
AALA335
AGLU372
AALA373
AALA375
AILE376
A3HC801
A3KK802
A5AD803
AHOH903
AHOH910
CGLY17
CHIS18
CASP19
CARG20
CGLY21
CVAL25
CGLY61
CVAL62
CSER63
CLEU65
CGLY67
CILE91
CALA92
CGLY93
CGLY94
CLEU113
CLEU114
CGLN115
CTHR117
CILE122
CHOH904
CHOH905
CHOH907
CHOH910
CHOH922
CHOH936
CHOH938

site_idAC7
Number of Residues37
DetailsBINDING SITE FOR RESIDUE B12 D 800
ChainResidue
BASP117
BPHE118
BMET120
BLEU123
BGLU140
BALA207
BGLN208
BGLU210
BGLU248
BALA249
BALA335
BGLU372
BALA373
BALA375
BILE376
B3HC801
B3KK802
DGLY17
DHIS18
DASP19
DARG20
DGLY21
DVAL25
DGLY61
DVAL62
DSER63
DLEU65
DGLY67
DILE91
DGLY93
DGLY94
DLEU113
DLEU114
DGLN115
DTHR117
DILE122
DHOH901

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:25720495, ECO:0007744|PDB:4R3U
ChainResidueDetails
CHIS18
DHIS18
BASP117
BTHR196
BARG235
BASN240
BHIS245
BARG284
AASP117
ATHR196
AARG235
AASN240
AHIS245
AARG284
BTYR76
BTHR86

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Important for the stereospecificity of catalysis => ECO:0000305|PubMed:25720495
ChainResidueDetails
AASP117
BASP117

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PDB entries from 2024-06-12

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