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6S6Y

X-ray crystal structure of the formyltransferase/hydrolase complex (FhcABCD) from Methylorubrum extorquens in complex with methylofuran

Functional Information from GO Data
ChainGOidnamespacecontents
A0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
C0015948biological_processmethanogenesis
C0016491molecular_functionoxidoreductase activity
C0018493molecular_functionformylmethanofuran dehydrogenase activity
C0046914molecular_functiontransition metal ion binding
D0006730biological_processone-carbon metabolic process
D0016740molecular_functiontransferase activity
D0030270molecular_functionformylmethanofuran-tetrahydromethanopterin N-formyltransferase activity
E0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
G0015948biological_processmethanogenesis
G0016491molecular_functionoxidoreductase activity
G0018493molecular_functionformylmethanofuran dehydrogenase activity
G0046914molecular_functiontransition metal ion binding
H0006730biological_processone-carbon metabolic process
H0016740molecular_functiontransferase activity
H0030270molecular_functionformylmethanofuran-tetrahydromethanopterin N-formyltransferase activity
I0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
K0015948biological_processmethanogenesis
K0016491molecular_functionoxidoreductase activity
K0018493molecular_functionformylmethanofuran dehydrogenase activity
K0046914molecular_functiontransition metal ion binding
L0006730biological_processone-carbon metabolic process
L0016740molecular_functiontransferase activity
L0030270molecular_functionformylmethanofuran-tetrahydromethanopterin N-formyltransferase activity
M0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
O0015948biological_processmethanogenesis
O0016491molecular_functionoxidoreductase activity
O0018493molecular_functionformylmethanofuran dehydrogenase activity
O0046914molecular_functiontransition metal ion binding
P0006730biological_processone-carbon metabolic process
P0016740molecular_functiontransferase activity
P0030270molecular_functionformylmethanofuran-tetrahydromethanopterin N-formyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue FMT A 601
ChainResidue
AASN64
ASER331

site_idAC2
Number of Residues11
Detailsbinding site for residue MFN A 602
ChainResidue
AGLN355
AASP377
AASN380
AZN605
AHIS229
ALEU233
AHIS258
APHE261
ATHR308
ASER310
ATYR345

site_idAC3
Number of Residues3
Detailsbinding site for residue GOL A 603
ChainResidue
APRO130
ATRP492
BARG42

site_idAC4
Number of Residues3
Detailsbinding site for residue ZN A 604
ChainResidue
AHIS59
AKCX176
AZN605

site_idAC5
Number of Residues5
Detailsbinding site for residue ZN A 605
ChainResidue
AKCX176
AHIS229
AHIS258
AMFN602
AZN604

site_idAC6
Number of Residues3
Detailsbinding site for residue CA A 606
ChainResidue
AGLU218
ILYS419
IGLU421

site_idAC7
Number of Residues2
Detailsbinding site for residue CA A 607
ChainResidue
AGLU398
AGLU423

site_idAC8
Number of Residues2
Detailsbinding site for residue CA A 608
ChainResidue
ASER117
AASP334

site_idAC9
Number of Residues1
Detailsbinding site for residue K A 609
ChainResidue
AASP463

site_idAD1
Number of Residues1
Detailsbinding site for residue K A 610
ChainResidue
AGLU399

site_idAD2
Number of Residues2
Detailsbinding site for residue CL A 611
ChainResidue
AGLU289
AARG371

site_idAD3
Number of Residues1
Detailsbinding site for residue CL A 612
ChainResidue
ALYS208

site_idAD4
Number of Residues3
Detailsbinding site for residue CA B 401
ChainResidue
BGLU66
BASP217
BARG222

site_idAD5
Number of Residues3
Detailsbinding site for residue CL C 301
ChainResidue
BARG251
CASP70
CARG71

site_idAD6
Number of Residues2
Detailsbinding site for residue K D 401
ChainResidue
DASP60
DLYS196

site_idAD7
Number of Residues4
Detailsbinding site for residue ZN E 601
ChainResidue
EKCX176
EHIS229
EHIS258
EZN602

site_idAD8
Number of Residues3
Detailsbinding site for residue ZN E 602
ChainResidue
EHIS59
EKCX176
EZN601

site_idAD9
Number of Residues6
Detailsbinding site for residue GOL H 401
ChainResidue
HVAL50
HGLU56
HPHE82
HGLY170
HGLY171
HASP256

site_idAE1
Number of Residues2
Detailsbinding site for residue K H 402
ChainResidue
HASP60
HLYS196

site_idAE2
Number of Residues2
Detailsbinding site for residue FMT I 601
ChainResidue
IASN64
IGLY337

site_idAE3
Number of Residues12
Detailsbinding site for residue L6K I 602
ChainResidue
IHIS229
ILEU233
IGLY234
IHIS258
IPHE261
ITHR308
IVAL351
IGLN355
IASP377
IASN380
IEDO603
IZN604

site_idAE4
Number of Residues3
Detailsbinding site for residue EDO I 603
ChainResidue
IARG315
IGLN316
IL6K602

site_idAE5
Number of Residues5
Detailsbinding site for residue ZN I 604
ChainResidue
IKCX176
IHIS229
IHIS258
IL6K602
IZN605

site_idAE6
Number of Residues3
Detailsbinding site for residue ZN I 605
ChainResidue
IHIS59
IKCX176
IZN604

site_idAE7
Number of Residues3
Detailsbinding site for residue K I 606
ChainResidue
AASP505
IASP396
IGLU423

site_idAE8
Number of Residues4
Detailsbinding site for residue CL I 607
ChainResidue
IGLY349
IPRO350
IVAL351
ISER352

site_idAE9
Number of Residues1
Detailsbinding site for residue FMT J 401
ChainResidue
JARG222

site_idAF1
Number of Residues4
Detailsbinding site for residue NA J 402
ChainResidue
JGLU37
JSER39
JGLY316
JALA317

site_idAF2
Number of Residues1
Detailsbinding site for residue K J 403
ChainResidue
JGLU191

site_idAF3
Number of Residues2
Detailsbinding site for residue CL J 404
ChainResidue
JARG251
KARG71

site_idAF4
Number of Residues2
Detailsbinding site for residue CA L 401
ChainResidue
LASP60
LLYS196

site_idAF5
Number of Residues1
Detailsbinding site for residue CA L 402
ChainResidue
LGLU189

site_idAF6
Number of Residues1
Detailsbinding site for residue K L 403
ChainResidue
LGLU155

site_idAF7
Number of Residues5
Detailsbinding site for residue ZN M 601
ChainResidue
MHIS59
MKCX176
MSER310
MLEU311
MZN602

site_idAF8
Number of Residues4
Detailsbinding site for residue ZN M 602
ChainResidue
MKCX176
MHIS229
MHIS258
MZN601

site_idAF9
Number of Residues4
Detailsbinding site for residue GLU O 303
ChainResidue
OILE178
OARG197
OARG198
OGLU302

site_idAG1
Number of Residues2
Detailsbinding site for residue K P 401
ChainResidue
PASP60
PLYS196

site_idAG2
Number of Residues1
Detailsbinding site for residue K P 402
ChainResidue
PGLU189

site_idAG3
Number of Residues16
Detailsbinding site for Di-peptide DGL B 402 and GLU C 304
ChainResidue
ALYS326
BALA3
BTRP4
BARG154
BARG202
BALA287
BALA296
BTHR300
BALA301
BVAL303
BILE305
BNH2403
CILE178
CARG197
CARG198
CGLU303

site_idAG4
Number of Residues5
Detailsbinding site for Di-peptide DGL B 402 and NH2 B 403
ChainResidue
ALYS326
BARG154
BARG202
CARG197
CGLU304

site_idAG5
Number of Residues12
Detailsbinding site for Di-peptide DGL C 302 and DGL D 402
ChainResidue
CGLU303
DGLU12
DTHR14
DARG124
DALA133
DTRP147
DTYR300
DHIS301
DARG303
DASP304
DLEU305
DIAS403

site_idAG6
Number of Residues13
Detailsbinding site for Di-peptide DGL C 302 and IAS D 403
ChainResidue
CARG160
CALA179
CGLU303
DGLU12
DTHR14
DARG135
DARG145
DTYR300
DHIS301
DARG303
DASP304
DLEU305
DDGL402

site_idAG7
Number of Residues3
Detailsbinding site for Di-peptide DGL C 302 and GLU C 303
ChainResidue
CGLU304
DDGL402
DIAS403

site_idAG8
Number of Residues10
Detailsbinding site for Di-peptide DGL I 608 and GLU L 404
ChainResidue
ILYS326
IARG400
IALA401
ILYS402
IGLU403
IALA405
ITHR406
ILEU407
ILEU417
KDGL301

site_idAG9
Number of Residues14
Detailsbinding site for Di-peptide GLU I 609 and DGL K 301
ChainResidue
IGLN260
IGLN300
IVAL302
ILYS326
IGLN355
ITRP356
IGLY381
IDGL610
JGLU405
KILE178
KARG197
KARG198
KGLU302
LGLU404

site_idAH1
Number of Residues13
Detailsbinding site for Di-peptide DGL I 610 and GLU J 405
ChainResidue
ILYS326
ITRP328
IALA401
ILYS402
IGLU403
IILE404
ITHR406
ILEU407
IGLU609
JGLY73
JARG154
JARG202
KARG197

site_idAH2
Number of Residues7
Detailsbinding site for Di-peptide DGL K 301 and GLU K 302
ChainResidue
IGLU609
KARG160
KARG161
KALA179
LGLU404
LDGL405
LDGL406

site_idAH3
Number of Residues11
Detailsbinding site for Di-peptide DGL K 301 and GLU L 404
ChainResidue
IDGL608
IGLU609
KGLU302
LTHR14
LPHE15
LHIS299
LTYR300
LLEU302
LARG303
LASP304
LLEU305

site_idAH4
Number of Residues17
Detailsbinding site for Di-peptide GLU K 302 and DGL L 406
ChainResidue
KARG160
KARG161
KALA179
KGLY180
KDGL301
LGLU12
LTHR14
LALA133
LLYS134
LARG135
LARG145
LTYR300
LHIS301
LARG303
LASP304
LLEU305
LDGL405

site_idAH5
Number of Residues16
Detailsbinding site for Di-peptide GLU K 302 and DGL L 405
ChainResidue
KARG160
KARG161
KALA179
KARG198
KDGL301
LGLU12
LTHR14
LARG124
LALA133
LTRP147
LTYR300
LHIS301
LARG303
LASP304
LLEU305
LDGL406

site_idAH6
Number of Residues14
Detailsbinding site for Di-peptide DGL O 301 and IAS P 404
ChainResidue
BGLU164
OGLU302
PTHR14
PPHE15
PALA133
PARG135
PARG145
PHIS299
PTYR300
PLEU302
PARG303
PASP304
PLEU305
PDGL403

site_idAH7
Number of Residues3
Detailsbinding site for Di-peptide DGL O 301 and GLU O 302
ChainResidue
OGLU303
PDGL403
PIAS404

site_idAH8
Number of Residues15
Detailsbinding site for Di-peptide DGL O 301 and DGL P 403
ChainResidue
BGLU164
OARG198
OLYS258
OGLU302
PTHR14
PPHE15
PARG124
PTRP147
PHIS299
PTYR300
PLEU302
PARG303
PASP304
PLEU305
PIAS404

Functional Information from PROSITE/UniProt
site_idPS01070
Number of Residues9
DetailsNUCLEASE_NON_SPEC DNA/RNA non-specific endonucleases active site. DRGHLregA
ChainResidueDetails
AASP445-ALA453

222415

PDB entries from 2024-07-10

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