Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5LMM

Structure of E coli Hydrogenase Hyd-1 mutant E28Q

Functional Information from GO Data
ChainGOidnamespacecontents
L0005515molecular_functionprotein binding
L0005886cellular_componentplasma membrane
L0006113biological_processfermentation
L0008901molecular_functionferredoxin hydrogenase activity
L0009055molecular_functionelectron transfer activity
L0009061biological_processanaerobic respiration
L0009267biological_processcellular response to starvation
L0016020cellular_componentmembrane
L0016151molecular_functionnickel cation binding
L0016491molecular_functionoxidoreductase activity
L0019645biological_processanaerobic electron transport chain
L0030288cellular_componentouter membrane-bounded periplasmic space
L0033748molecular_functionhydrogenase (acceptor) activity
L0044569cellular_component[Ni-Fe] hydrogenase complex
L0046872molecular_functionmetal ion binding
L0098567cellular_componentperiplasmic side of plasma membrane
L1902421biological_processhydrogen metabolic process
M0005515molecular_functionprotein binding
M0005886cellular_componentplasma membrane
M0006113biological_processfermentation
M0008901molecular_functionferredoxin hydrogenase activity
M0009055molecular_functionelectron transfer activity
M0009061biological_processanaerobic respiration
M0009267biological_processcellular response to starvation
M0016020cellular_componentmembrane
M0016151molecular_functionnickel cation binding
M0016491molecular_functionoxidoreductase activity
M0019645biological_processanaerobic electron transport chain
M0030288cellular_componentouter membrane-bounded periplasmic space
M0033748molecular_functionhydrogenase (acceptor) activity
M0044569cellular_component[Ni-Fe] hydrogenase complex
M0046872molecular_functionmetal ion binding
M0098567cellular_componentperiplasmic side of plasma membrane
M1902421biological_processhydrogen metabolic process
S0005515molecular_functionprotein binding
S0005886cellular_componentplasma membrane
S0006113biological_processfermentation
S0008901molecular_functionferredoxin hydrogenase activity
S0009055molecular_functionelectron transfer activity
S0009061biological_processanaerobic respiration
S0009267biological_processcellular response to starvation
S0009375cellular_componentferredoxin hydrogenase complex
S0016020cellular_componentmembrane
S0016491molecular_functionoxidoreductase activity
S0019645biological_processanaerobic electron transport chain
S0033748molecular_functionhydrogenase (acceptor) activity
S0044569cellular_component[Ni-Fe] hydrogenase complex
S0046872molecular_functionmetal ion binding
S0051536molecular_functioniron-sulfur cluster binding
S0051538molecular_function3 iron, 4 sulfur cluster binding
S0051539molecular_function4 iron, 4 sulfur cluster binding
S0098567cellular_componentperiplasmic side of plasma membrane
S1902421biological_processhydrogen metabolic process
T0005515molecular_functionprotein binding
T0005886cellular_componentplasma membrane
T0006113biological_processfermentation
T0008901molecular_functionferredoxin hydrogenase activity
T0009055molecular_functionelectron transfer activity
T0009061biological_processanaerobic respiration
T0009267biological_processcellular response to starvation
T0009375cellular_componentferredoxin hydrogenase complex
T0016020cellular_componentmembrane
T0016491molecular_functionoxidoreductase activity
T0019645biological_processanaerobic electron transport chain
T0033748molecular_functionhydrogenase (acceptor) activity
T0044569cellular_component[Ni-Fe] hydrogenase complex
T0046872molecular_functionmetal ion binding
T0051536molecular_functioniron-sulfur cluster binding
T0051538molecular_function3 iron, 4 sulfur cluster binding
T0051539molecular_function4 iron, 4 sulfur cluster binding
T0098567cellular_componentperiplasmic side of plasma membrane
T1902421biological_processhydrogen metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue SF4 S 401
ChainResidue
SHIS187
SCYS190
SARG193
SCYS215
SLEU216
SCYS221
SILE243

site_idAC2
Number of Residues8
Detailsbinding site for residue F3S S 402
ChainResidue
SASN228
SCYS230
STRP235
SCYS249
SLEU250
SCYS252
LLYS226
STHR226

site_idAC3
Number of Residues13
Detailsbinding site for residue SF3 S 403
ChainResidue
LHOH726
SGLU16
SCYS17
STHR18
SCYS19
SCYS20
SGLU76
STHR114
SCYS115
SCYS120
SGLY148
SCYS149
SHOH526

site_idAC4
Number of Residues4
Detailsbinding site for residue LMT S 404
ChainResidue
SILE7
STRP11
SMET163
SHOH678

site_idAC5
Number of Residues4
Detailsbinding site for residue CL S 405
ChainResidue
STRP118
SCYS120
SGLY256
SHOH604

site_idAC6
Number of Residues8
Detailsbinding site for residue SO4 S 406
ChainResidue
MARG355
MTRP373
MHOH1094
SARG125
SPRO126
SHOH510
SHOH557
SHOH671

site_idAC7
Number of Residues3
Detailsbinding site for residue SO4 L 601
ChainResidue
LLEU482
LALA483
SARG211

site_idAC8
Number of Residues13
Detailsbinding site for residue FCO L 602
ChainResidue
LCSO79
LVAL82
LHIS83
LALA507
LPRO508
LARG509
LLEU512
LVAL530
LPRO531
LTHR532
LCYS579
LNI603
LHOH1030

site_idAC9
Number of Residues6
Detailsbinding site for residue NI L 603
ChainResidue
LCYS76
LCSO79
LCYS576
LCYS579
LFCO602
LHOH1030

site_idAD1
Number of Residues6
Detailsbinding site for residue MG L 604
ChainResidue
LGLU57
LCYS528
LHIS582
LHOH735
LHOH748
LHOH749

site_idAD2
Number of Residues5
Detailsbinding site for residue LI L 605
ChainResidue
LILE97
LHOH826
LHOH908
LHOH986
LHOH1099

site_idAD3
Number of Residues6
Detailsbinding site for residue SF4 T 401
ChainResidue
THIS187
TCYS190
TARG193
TCYS215
TLEU216
TCYS221

site_idAD4
Number of Residues9
Detailsbinding site for residue F3S T 402
ChainResidue
MLYS226
TTHR226
TASN228
TCYS230
TTRP235
TPRO242
TCYS249
TLEU250
TCYS252

site_idAD5
Number of Residues13
Detailsbinding site for residue SF3 T 403
ChainResidue
TTHR114
TCYS115
TCYS120
TGLY148
TCYS149
THOH555
MHOH717
TGLU16
TCYS17
TTHR18
TCYS19
TCYS20
TGLU76

site_idAD6
Number of Residues3
Detailsbinding site for residue LMT T 404
ChainResidue
TILE7
TTRP11
TMET163

site_idAD7
Number of Residues5
Detailsbinding site for residue CL T 405
ChainResidue
TTRP118
TCYS120
TGLY256
THOH631
THOH682

site_idAD8
Number of Residues5
Detailsbinding site for residue CL T 406
ChainResidue
TILE12
THIS13
TASP46
THOH579
THOH655

site_idAD9
Number of Residues2
Detailsbinding site for residue SO4 T 407
ChainResidue
TASP173
TARG174

site_idAE1
Number of Residues13
Detailsbinding site for residue FCO M 601
ChainResidue
MCSO79
MVAL82
MHIS83
MALA507
MPRO508
MARG509
MLEU512
MVAL530
MPRO531
MTHR532
MCYS579
MNI602
MHOH994

site_idAE2
Number of Residues6
Detailsbinding site for residue NI M 602
ChainResidue
MCYS76
MCSO79
MCYS576
MCYS579
MFCO601
MHOH994

site_idAE3
Number of Residues6
Detailsbinding site for residue MG M 603
ChainResidue
MGLU57
MCYS528
MHIS582
MHOH726
MHOH727
MHOH729

site_idAE4
Number of Residues3
Detailsbinding site for residue SO4 M 604
ChainResidue
MARG394
MHOH704
SARG125

site_idAE5
Number of Residues4
Detailsbinding site for residue LI M 605
ChainResidue
MHOH810
MHOH889
MHOH932
MHOH1110

site_idAE6
Number of Residues8
Detailsbinding site for residue TRS M 606
ChainResidue
MASP350
MASP359
MGLN392
MGLU393
MARG394
MHOH704
MHOH728
MHOH867

Functional Information from PROSITE/UniProt
site_idPS00507
Number of Residues26
DetailsNI_HGENASE_L_1 Nickel-dependent hydrogenases large subunit signature 1. RGLEiilqgrdprdawafvERiCGVC
ChainResidueDetails
LARG54-CSO79

site_idPS00508
Number of Residues10
DetailsNI_HGENASE_L_2 Nickel-dependent hydrogenases large subunit signature 2. FDPCLACst.H
ChainResidueDetails
LPHE573-HIS582

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255
ChainResidueDetails
LCYS76
LCSO79
LCYS576
LCYS579
MCYS76
MCSO79
MCYS576
MCYS579

site_idSWS_FT_FI2
Number of Residues84
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
SVAL282-ALA302
TVAL282-ALA302
STHR281-VAL303
TTHR281-VAL303

site_idSWS_FT_FI3
Number of Residues94
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
SVAL303-ALA327
TVAL303-ALA327
SASP304-ALA327
TASP304-ALA327

site_idSWS_FT_FI4
Number of Residues22
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P21853
ChainResidueDetails
SCYS230
SCYS249
SCYS252
TCYS17
TCYS20
TCYS115
TCYS149
THIS187
TCYS190
TCYS215
TCYS221
TCYS230
TCYS249
TCYS252
SCYS17
SCYS20
SCYS115
SCYS149
SHIS187
SCYS190
SCYS215
SCYS221

218500

PDB entries from 2024-04-17

PDB statisticsPDBj update infoContact PDBjnumon