1NBM
THE STRUCTURE OF BOVINE F1-ATPASE COVALENTLY INHIBITED WITH 4-CHLORO-7-NITROBENZOFURAZAN
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0005515 | molecular_function | protein binding |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005739 | cellular_component | mitochondrion |
A | 0005743 | cellular_component | mitochondrial inner membrane |
A | 0005753 | cellular_component | mitochondrial proton-transporting ATP synthase complex |
A | 0005754 | cellular_component | mitochondrial proton-transporting ATP synthase, catalytic core |
A | 0005886 | cellular_component | plasma membrane |
A | 0006754 | biological_process | ATP biosynthetic process |
A | 0006811 | biological_process | monoatomic ion transport |
A | 0015986 | biological_process | proton motive force-driven ATP synthesis |
A | 0016020 | cellular_component | membrane |
A | 0032559 | molecular_function | adenyl ribonucleotide binding |
A | 0043531 | molecular_function | ADP binding |
A | 0045261 | cellular_component | proton-transporting ATP synthase complex, catalytic core F(1) |
A | 0046034 | biological_process | ATP metabolic process |
A | 0046933 | molecular_function | proton-transporting ATP synthase activity, rotational mechanism |
A | 1902600 | biological_process | proton transmembrane transport |
B | 0000166 | molecular_function | nucleotide binding |
B | 0005515 | molecular_function | protein binding |
B | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005739 | cellular_component | mitochondrion |
B | 0005743 | cellular_component | mitochondrial inner membrane |
B | 0005753 | cellular_component | mitochondrial proton-transporting ATP synthase complex |
B | 0005754 | cellular_component | mitochondrial proton-transporting ATP synthase, catalytic core |
B | 0005886 | cellular_component | plasma membrane |
B | 0006754 | biological_process | ATP biosynthetic process |
B | 0006811 | biological_process | monoatomic ion transport |
B | 0015986 | biological_process | proton motive force-driven ATP synthesis |
B | 0016020 | cellular_component | membrane |
B | 0032559 | molecular_function | adenyl ribonucleotide binding |
B | 0043531 | molecular_function | ADP binding |
B | 0045261 | cellular_component | proton-transporting ATP synthase complex, catalytic core F(1) |
B | 0046034 | biological_process | ATP metabolic process |
B | 0046933 | molecular_function | proton-transporting ATP synthase activity, rotational mechanism |
B | 1902600 | biological_process | proton transmembrane transport |
C | 0000166 | molecular_function | nucleotide binding |
C | 0005515 | molecular_function | protein binding |
C | 0005524 | molecular_function | ATP binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0005739 | cellular_component | mitochondrion |
C | 0005743 | cellular_component | mitochondrial inner membrane |
C | 0005753 | cellular_component | mitochondrial proton-transporting ATP synthase complex |
C | 0005754 | cellular_component | mitochondrial proton-transporting ATP synthase, catalytic core |
C | 0005886 | cellular_component | plasma membrane |
C | 0006754 | biological_process | ATP biosynthetic process |
C | 0006811 | biological_process | monoatomic ion transport |
C | 0015986 | biological_process | proton motive force-driven ATP synthesis |
C | 0016020 | cellular_component | membrane |
C | 0032559 | molecular_function | adenyl ribonucleotide binding |
C | 0043531 | molecular_function | ADP binding |
C | 0045261 | cellular_component | proton-transporting ATP synthase complex, catalytic core F(1) |
C | 0046034 | biological_process | ATP metabolic process |
C | 0046933 | molecular_function | proton-transporting ATP synthase activity, rotational mechanism |
C | 1902600 | biological_process | proton transmembrane transport |
D | 0000166 | molecular_function | nucleotide binding |
D | 0005515 | molecular_function | protein binding |
D | 0005524 | molecular_function | ATP binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0005739 | cellular_component | mitochondrion |
D | 0005743 | cellular_component | mitochondrial inner membrane |
D | 0005753 | cellular_component | mitochondrial proton-transporting ATP synthase complex |
D | 0006754 | biological_process | ATP biosynthetic process |
D | 0006811 | biological_process | monoatomic ion transport |
D | 0015986 | biological_process | proton motive force-driven ATP synthesis |
D | 0016020 | cellular_component | membrane |
D | 0016887 | molecular_function | ATP hydrolysis activity |
D | 0042776 | biological_process | proton motive force-driven mitochondrial ATP synthesis |
D | 0045261 | cellular_component | proton-transporting ATP synthase complex, catalytic core F(1) |
D | 0046034 | biological_process | ATP metabolic process |
D | 0046933 | molecular_function | proton-transporting ATP synthase activity, rotational mechanism |
D | 0046961 | molecular_function | proton-transporting ATPase activity, rotational mechanism |
D | 1902600 | biological_process | proton transmembrane transport |
E | 0000166 | molecular_function | nucleotide binding |
E | 0005515 | molecular_function | protein binding |
E | 0005524 | molecular_function | ATP binding |
E | 0005737 | cellular_component | cytoplasm |
E | 0005739 | cellular_component | mitochondrion |
E | 0005743 | cellular_component | mitochondrial inner membrane |
E | 0005753 | cellular_component | mitochondrial proton-transporting ATP synthase complex |
E | 0006754 | biological_process | ATP biosynthetic process |
E | 0006811 | biological_process | monoatomic ion transport |
E | 0015986 | biological_process | proton motive force-driven ATP synthesis |
E | 0016020 | cellular_component | membrane |
E | 0016887 | molecular_function | ATP hydrolysis activity |
E | 0042776 | biological_process | proton motive force-driven mitochondrial ATP synthesis |
E | 0045261 | cellular_component | proton-transporting ATP synthase complex, catalytic core F(1) |
E | 0046034 | biological_process | ATP metabolic process |
E | 0046933 | molecular_function | proton-transporting ATP synthase activity, rotational mechanism |
E | 0046961 | molecular_function | proton-transporting ATPase activity, rotational mechanism |
E | 1902600 | biological_process | proton transmembrane transport |
F | 0000166 | molecular_function | nucleotide binding |
F | 0005515 | molecular_function | protein binding |
F | 0005524 | molecular_function | ATP binding |
F | 0005737 | cellular_component | cytoplasm |
F | 0005739 | cellular_component | mitochondrion |
F | 0005743 | cellular_component | mitochondrial inner membrane |
F | 0005753 | cellular_component | mitochondrial proton-transporting ATP synthase complex |
F | 0006754 | biological_process | ATP biosynthetic process |
F | 0006811 | biological_process | monoatomic ion transport |
F | 0015986 | biological_process | proton motive force-driven ATP synthesis |
F | 0016020 | cellular_component | membrane |
F | 0016887 | molecular_function | ATP hydrolysis activity |
F | 0042776 | biological_process | proton motive force-driven mitochondrial ATP synthesis |
F | 0045261 | cellular_component | proton-transporting ATP synthase complex, catalytic core F(1) |
F | 0046034 | biological_process | ATP metabolic process |
F | 0046933 | molecular_function | proton-transporting ATP synthase activity, rotational mechanism |
F | 0046961 | molecular_function | proton-transporting ATPase activity, rotational mechanism |
F | 1902600 | biological_process | proton transmembrane transport |
G | 0000275 | cellular_component | mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1) |
G | 0005515 | molecular_function | protein binding |
G | 0005739 | cellular_component | mitochondrion |
G | 0005743 | cellular_component | mitochondrial inner membrane |
G | 0005753 | cellular_component | mitochondrial proton-transporting ATP synthase complex |
G | 0006754 | biological_process | ATP biosynthetic process |
G | 0006811 | biological_process | monoatomic ion transport |
G | 0015986 | biological_process | proton motive force-driven ATP synthesis |
G | 0016020 | cellular_component | membrane |
G | 0045261 | cellular_component | proton-transporting ATP synthase complex, catalytic core F(1) |
G | 0046933 | molecular_function | proton-transporting ATP synthase activity, rotational mechanism |
G | 1902600 | biological_process | proton transmembrane transport |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG A 601 |
Chain | Residue |
A | THR176 |
A | GLN208 |
A | ASP269 |
A | ATP600 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG B 601 |
Chain | Residue |
B | THR176 |
B | GLN208 |
B | ASP269 |
B | ATP600 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG C 601 |
Chain | Residue |
C | THR176 |
C | ASP269 |
C | ATP600 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG D 601 |
Chain | Residue |
D | THR163 |
D | ADP600 |
D | HOH603 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PO4 E 602 |
Chain | Residue |
E | ALA158 |
E | GLY159 |
E | VAL160 |
E | GLY161 |
E | LYS162 |
E | THR163 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG F 601 |
Chain | Residue |
F | THR163 |
F | GLU188 |
F | GLU192 |
F | ATP600 |
site_id | AC7 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE ATP A 600 |
Chain | Residue |
A | GLN172 |
A | THR173 |
A | GLY174 |
A | LYS175 |
A | THR176 |
A | SER177 |
A | PHE357 |
A | ARG362 |
A | GLN430 |
A | GLN432 |
A | MG601 |
A | HOH606 |
D | ARG372 |
site_id | AC8 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE ATP B 600 |
Chain | Residue |
B | ASP170 |
B | ARG171 |
B | GLN172 |
B | THR173 |
B | GLY174 |
B | LYS175 |
B | THR176 |
B | SER177 |
B | PHE357 |
B | ARG362 |
B | GLN430 |
B | GLN432 |
B | MG601 |
B | HOH610 |
B | HOH615 |
E | ASP359 |
site_id | AC9 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE ATP C 600 |
Chain | Residue |
C | GLN172 |
C | THR173 |
C | GLY174 |
C | LYS175 |
C | THR176 |
C | SER177 |
C | PHE357 |
C | PRO363 |
C | GLN430 |
C | GLY431 |
C | GLN432 |
C | MG601 |
C | HOH602 |
C | HOH611 |
site_id | BC1 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE ADP D 600 |
Chain | Residue |
C | SER372 |
C | ARG373 |
D | GLY157 |
D | ALA158 |
D | GLY159 |
D | VAL160 |
D | GLY161 |
D | LYS162 |
D | THR163 |
D | VAL164 |
D | TYR345 |
D | PHE418 |
D | ALA421 |
D | PHE424 |
D | THR425 |
D | MG601 |
D | HOH603 |
D | HOH610 |
site_id | BC2 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE ATP F 600 |
Chain | Residue |
B | ARG373 |
F | GLY157 |
F | GLY159 |
F | VAL160 |
F | GLY161 |
F | LYS162 |
F | THR163 |
F | VAL164 |
F | GLU188 |
F | ARG189 |
F | TYR345 |
F | PHE418 |
F | ALA421 |
F | PHE424 |
F | THR425 |
F | MG601 |
F | HOH609 |
B | SER344 |
B | VAL371 |
site_id | CA1 |
Number of Residues | 2 |
Details | THE CARBOXYLATE GROUP OF THE GLUTAMIC ACID RESIDUE IS BELIEVED TO ACTIVATE A WATER MOLECULE FOR INLINE ATTACK ON THE GAMMA PHOSPHATE DURING ATP HYDROLYSIS. THE ARGININE RESIDUE (WHICH IS LOCATED ON AN ADJACENT ALPHA SUBUNIT) COULD HELP TO STABLISE THE NEGATIVE CHARGE THAT DEVELOPS ON THE TERMINAL PHOSPHATE IN THE PUTATIVE PENTACOORDINATED TRANSITION STATE. |
Chain | Residue |
D | GLU188 |
C | ARG373 |
site_id | CA2 |
Number of Residues | 2 |
Details | THE CARBOXYLATE GROUP OF THE GLUTAMIC ACID RESIDUE IS BELIEVED TO ACTIVATE A WATER MOLECULE FOR INLINE ATTACK ON THE GAMMA PHOSPHATE DURING ATP HYDROLYSIS. THE ARGININE RESIDUE (WHICH IS LOCATED ON AN ADJACENT ALPHA SUBUNIT) COULD HELP TO STABLISE THE NEGATIVE CHARGE THAT DEVELOPS ON THE TERMINAL PHOSPHATE IN THE PUTATIVE PENTACOORDINATED TRANSITION STATE. |
Chain | Residue |
A | ARG373 |
E | GLU188 |
site_id | CA3 |
Number of Residues | 2 |
Details | THE CARBOXYLATE GROUP OF THE GLUTAMIC ACID RESIDUE IS BELIEVED TO ACTIVATE A WATER MOLECULE FOR INLINE ATTACK ON THE GAMMA PHOSPHATE DURING ATP HYDROLYSIS. THE ARGININE RESIDUE (WHICH IS LOCATED ON AN ADJACENT ALPHA SUBUNIT) COULD HELP TO STABLISE THE NEGATIVE CHARGE THAT DEVELOPS ON THE TERMINAL PHOSPHATE IN THE PUTATIVE PENTACOORDINATED TRANSITION STATE. |
Chain | Residue |
F | GLU188 |
B | ARG373 |
site_id | PL1 |
Number of Residues | 1 |
Details | THE RESIDUE LISTED IS THE LYSINE WITHIN THE P-LOOP (PHOSPHATE BINDING) MOTIF, GXXXXGKT/S. |
Chain | Residue |
A | LYS175 |
site_id | PL2 |
Number of Residues | 1 |
Details | THE RESIDUE LISTED IS THE LYSINE WITHIN THE P-LOOP (PHOSPHATE BINDING) MOTIF, GXXXXGKT/S. |
Chain | Residue |
B | LYS175 |
site_id | PL3 |
Number of Residues | 1 |
Details | THE RESIDUE LISTED IS THE LYSINE WITHIN THE P-LOOP (PHOSPHATE BINDING) MOTIF, GXXXXGKT/S. |
Chain | Residue |
C | LYS175 |
site_id | PL4 |
Number of Residues | 1 |
Details | THE RESIDUE LISTED IS THE LYSINE WITHIN THE P-LOOP (PHOSPHATE BINDING) MOTIF, GXXXXGKT/S. |
Chain | Residue |
D | LYS162 |
site_id | PL5 |
Number of Residues | 1 |
Details | THE RESIDUE LISTED IS THE LYSINE WITHIN THE P-LOOP (PHOSPHATE BINDING) MOTIF, GXXXXGKT/S. |
Chain | Residue |
E | LYS162 |
site_id | PL6 |
Number of Residues | 1 |
Details | THE RESIDUE LISTED IS THE LYSINE WITHIN THE P-LOOP (PHOSPHATE BINDING) MOTIF, GXXXXGKT/S. |
Chain | Residue |
F | LYS162 |
Functional Information from PROSITE/UniProt
site_id | PS00153 |
Number of Residues | 14 |
Details | ATPASE_GAMMA ATP synthase gamma subunit signature. ITkEliEiisGAaA |
Chain | Residue | Details |
G | ILE258-ALA271 |
site_id | PS00152 |
Number of Residues | 10 |
Details | ATPASE_ALPHA_BETA ATP synthase alpha and beta subunits signature. PAINVGLSVS |
Chain | Residue | Details |
A | PRO363-SER372 | |
E | PRO346-SER355 | |
D | PRO346-SER355 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q91VR2 |
Chain | Residue | Details |
G | LYS14 | |
F | GLY157 | |
B | ASP170 | |
B | GLN430 | |
C | ASP170 | |
C | GLN430 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q91VR2 |
Chain | Residue | Details |
G | LYS24 | |
G | LYS245 | |
C | SER370 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P36542 |
Chain | Residue | Details |
G | LYS30 | |
F | LYS472 | |
G | LYS172 | |
E | LYS209 | |
E | LYS214 | |
E | LYS472 | |
F | LYS74 | |
F | LYS111 | |
F | LYS209 | |
F | LYS214 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 |
Chain | Residue | Details |
G | LYS90 | |
C | SER22 | |
C | SER123 | |
C | SER141 | |
G | LYS129 | |
F | LYS148 | |
F | LYS376 | |
B | SER10 | |
B | SER22 | |
B | SER123 | |
B | SER141 | |
C | SER10 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P36542 |
Chain | Residue | Details |
G | SER121 | |
F | THR262 | |
C | SER33 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P06576 |
Chain | Residue | Details |
E | SER365 | |
F | SER365 | |
C | SER63 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P10719 |
Chain | Residue | Details |
E | SER383 | |
B | LYS498 | |
C | LYS80 | |
C | LYS83 | |
C | LYS89 | |
C | LYS197 | |
C | LYS498 | |
F | SER383 | |
A | LYS89 | |
A | LYS197 | |
A | LYS498 | |
B | LYS80 | |
B | LYS83 | |
B | LYS89 | |
B | LYS197 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P56480 |
Chain | Residue | Details |
E | LYS430 | |
E | LYS435 | |
F | LYS430 | |
F | LYS435 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | CARBOHYD: O-linked (GlcNAc) serine => ECO:0000250 |
Chain | Residue | Details |
E | SER56 | |
A | LYS488 | |
A | LYS496 | |
B | LYS118 | |
B | LYS124 | |
B | LYS187 | |
B | LYS196 | |
B | LYS218 | |
B | LYS262 | |
B | LYS384 | |
B | LYS455 | |
F | SER56 | |
B | LYS463 | |
B | LYS488 | |
B | LYS496 | |
C | LYS118 | |
C | LYS124 | |
C | LYS187 | |
C | LYS196 | |
C | LYS218 | |
C | LYS262 | |
C | LYS384 | |
A | LYS187 | |
C | LYS455 | |
C | LYS463 | |
C | LYS488 | |
C | LYS496 | |
A | LYS196 | |
A | LYS218 | |
A | LYS262 | |
A | LYS384 | |
A | LYS455 | |
A | LYS463 |
site_id | SWS_FT_FI10 |
Number of Residues | 3 |
Details | MOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:Q03265 |
Chain | Residue | Details |
A | ARG161 | |
B | ARG161 | |
C | ARG161 |
site_id | SWS_FT_FI11 |
Number of Residues | 3 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P25705 |
Chain | Residue | Details |
A | LYS391 | |
B | LYS391 | |
C | LYS391 |
site_id | SWS_FT_FI12 |
Number of Residues | 3 |
Details | CARBOHYD: O-linked (GlcNAc) serine; alternate => ECO:0000250 |
Chain | Residue | Details |
A | SER33 | |
B | SER33 | |
C | SER33 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 3 |
Details | M-CSA 178 |
Chain | Residue | Details |
E | LYS162 | electrostatic stabiliser |
E | GLU188 | electrostatic stabiliser |
E | ARG189 | electrostatic stabiliser |
site_id | MCSA2 |
Number of Residues | 3 |
Details | M-CSA 178 |
Chain | Residue | Details |
F | LYS162 | electrostatic stabiliser |
F | GLU188 | electrostatic stabiliser |
F | ARG189 | electrostatic stabiliser |
site_id | MCSA3 |
Number of Residues | 1 |
Details | M-CSA 178 |
Chain | Residue | Details |
C | ARG373 | electrostatic stabiliser |