4OKN
Crystal structure of human muscle L-lactate dehydrogenase, ternary complex with NADH and oxalate
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004457 | molecular_function | lactate dehydrogenase activity |
A | 0004459 | molecular_function | L-lactate dehydrogenase (NAD+) activity |
A | 0005515 | molecular_function | protein binding |
A | 0005634 | cellular_component | nucleus |
A | 0005737 | cellular_component | cytoplasm |
A | 0005739 | cellular_component | mitochondrion |
A | 0005829 | cellular_component | cytosol |
A | 0006089 | biological_process | lactate metabolic process |
A | 0006096 | biological_process | glycolytic process |
A | 0016020 | cellular_component | membrane |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
A | 0019661 | biological_process | glucose catabolic process to lactate via pyruvate |
A | 0019752 | biological_process | carboxylic acid metabolic process |
A | 0035686 | cellular_component | sperm fibrous sheath |
A | 0042802 | molecular_function | identical protein binding |
A | 0042867 | biological_process | pyruvate catabolic process |
A | 0045296 | molecular_function | cadherin binding |
A | 0070062 | cellular_component | extracellular exosome |
A | 1990204 | cellular_component | oxidoreductase complex |
B | 0003824 | molecular_function | catalytic activity |
B | 0004457 | molecular_function | lactate dehydrogenase activity |
B | 0004459 | molecular_function | L-lactate dehydrogenase (NAD+) activity |
B | 0005515 | molecular_function | protein binding |
B | 0005634 | cellular_component | nucleus |
B | 0005737 | cellular_component | cytoplasm |
B | 0005739 | cellular_component | mitochondrion |
B | 0005829 | cellular_component | cytosol |
B | 0006089 | biological_process | lactate metabolic process |
B | 0006096 | biological_process | glycolytic process |
B | 0016020 | cellular_component | membrane |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
B | 0019661 | biological_process | glucose catabolic process to lactate via pyruvate |
B | 0019752 | biological_process | carboxylic acid metabolic process |
B | 0035686 | cellular_component | sperm fibrous sheath |
B | 0042802 | molecular_function | identical protein binding |
B | 0042867 | biological_process | pyruvate catabolic process |
B | 0045296 | molecular_function | cadherin binding |
B | 0070062 | cellular_component | extracellular exosome |
B | 1990204 | cellular_component | oxidoreductase complex |
C | 0003824 | molecular_function | catalytic activity |
C | 0004457 | molecular_function | lactate dehydrogenase activity |
C | 0004459 | molecular_function | L-lactate dehydrogenase (NAD+) activity |
C | 0005515 | molecular_function | protein binding |
C | 0005634 | cellular_component | nucleus |
C | 0005737 | cellular_component | cytoplasm |
C | 0005739 | cellular_component | mitochondrion |
C | 0005829 | cellular_component | cytosol |
C | 0006089 | biological_process | lactate metabolic process |
C | 0006096 | biological_process | glycolytic process |
C | 0016020 | cellular_component | membrane |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
C | 0019661 | biological_process | glucose catabolic process to lactate via pyruvate |
C | 0019752 | biological_process | carboxylic acid metabolic process |
C | 0035686 | cellular_component | sperm fibrous sheath |
C | 0042802 | molecular_function | identical protein binding |
C | 0042867 | biological_process | pyruvate catabolic process |
C | 0045296 | molecular_function | cadherin binding |
C | 0070062 | cellular_component | extracellular exosome |
C | 1990204 | cellular_component | oxidoreductase complex |
D | 0003824 | molecular_function | catalytic activity |
D | 0004457 | molecular_function | lactate dehydrogenase activity |
D | 0004459 | molecular_function | L-lactate dehydrogenase (NAD+) activity |
D | 0005515 | molecular_function | protein binding |
D | 0005634 | cellular_component | nucleus |
D | 0005737 | cellular_component | cytoplasm |
D | 0005739 | cellular_component | mitochondrion |
D | 0005829 | cellular_component | cytosol |
D | 0006089 | biological_process | lactate metabolic process |
D | 0006096 | biological_process | glycolytic process |
D | 0016020 | cellular_component | membrane |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
D | 0019661 | biological_process | glucose catabolic process to lactate via pyruvate |
D | 0019752 | biological_process | carboxylic acid metabolic process |
D | 0035686 | cellular_component | sperm fibrous sheath |
D | 0042802 | molecular_function | identical protein binding |
D | 0042867 | biological_process | pyruvate catabolic process |
D | 0045296 | molecular_function | cadherin binding |
D | 0070062 | cellular_component | extracellular exosome |
D | 1990204 | cellular_component | oxidoreductase complex |
E | 0003824 | molecular_function | catalytic activity |
E | 0004457 | molecular_function | lactate dehydrogenase activity |
E | 0004459 | molecular_function | L-lactate dehydrogenase (NAD+) activity |
E | 0005515 | molecular_function | protein binding |
E | 0005634 | cellular_component | nucleus |
E | 0005737 | cellular_component | cytoplasm |
E | 0005739 | cellular_component | mitochondrion |
E | 0005829 | cellular_component | cytosol |
E | 0006089 | biological_process | lactate metabolic process |
E | 0006096 | biological_process | glycolytic process |
E | 0016020 | cellular_component | membrane |
E | 0016491 | molecular_function | oxidoreductase activity |
E | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
E | 0019661 | biological_process | glucose catabolic process to lactate via pyruvate |
E | 0019752 | biological_process | carboxylic acid metabolic process |
E | 0035686 | cellular_component | sperm fibrous sheath |
E | 0042802 | molecular_function | identical protein binding |
E | 0042867 | biological_process | pyruvate catabolic process |
E | 0045296 | molecular_function | cadherin binding |
E | 0070062 | cellular_component | extracellular exosome |
E | 1990204 | cellular_component | oxidoreductase complex |
F | 0003824 | molecular_function | catalytic activity |
F | 0004457 | molecular_function | lactate dehydrogenase activity |
F | 0004459 | molecular_function | L-lactate dehydrogenase (NAD+) activity |
F | 0005515 | molecular_function | protein binding |
F | 0005634 | cellular_component | nucleus |
F | 0005737 | cellular_component | cytoplasm |
F | 0005739 | cellular_component | mitochondrion |
F | 0005829 | cellular_component | cytosol |
F | 0006089 | biological_process | lactate metabolic process |
F | 0006096 | biological_process | glycolytic process |
F | 0016020 | cellular_component | membrane |
F | 0016491 | molecular_function | oxidoreductase activity |
F | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
F | 0019661 | biological_process | glucose catabolic process to lactate via pyruvate |
F | 0019752 | biological_process | carboxylic acid metabolic process |
F | 0035686 | cellular_component | sperm fibrous sheath |
F | 0042802 | molecular_function | identical protein binding |
F | 0042867 | biological_process | pyruvate catabolic process |
F | 0045296 | molecular_function | cadherin binding |
F | 0070062 | cellular_component | extracellular exosome |
F | 1990204 | cellular_component | oxidoreductase complex |
G | 0003824 | molecular_function | catalytic activity |
G | 0004457 | molecular_function | lactate dehydrogenase activity |
G | 0004459 | molecular_function | L-lactate dehydrogenase (NAD+) activity |
G | 0005515 | molecular_function | protein binding |
G | 0005634 | cellular_component | nucleus |
G | 0005737 | cellular_component | cytoplasm |
G | 0005739 | cellular_component | mitochondrion |
G | 0005829 | cellular_component | cytosol |
G | 0006089 | biological_process | lactate metabolic process |
G | 0006096 | biological_process | glycolytic process |
G | 0016020 | cellular_component | membrane |
G | 0016491 | molecular_function | oxidoreductase activity |
G | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
G | 0019661 | biological_process | glucose catabolic process to lactate via pyruvate |
G | 0019752 | biological_process | carboxylic acid metabolic process |
G | 0035686 | cellular_component | sperm fibrous sheath |
G | 0042802 | molecular_function | identical protein binding |
G | 0042867 | biological_process | pyruvate catabolic process |
G | 0045296 | molecular_function | cadherin binding |
G | 0070062 | cellular_component | extracellular exosome |
G | 1990204 | cellular_component | oxidoreductase complex |
H | 0003824 | molecular_function | catalytic activity |
H | 0004457 | molecular_function | lactate dehydrogenase activity |
H | 0004459 | molecular_function | L-lactate dehydrogenase (NAD+) activity |
H | 0005515 | molecular_function | protein binding |
H | 0005634 | cellular_component | nucleus |
H | 0005737 | cellular_component | cytoplasm |
H | 0005739 | cellular_component | mitochondrion |
H | 0005829 | cellular_component | cytosol |
H | 0006089 | biological_process | lactate metabolic process |
H | 0006096 | biological_process | glycolytic process |
H | 0016020 | cellular_component | membrane |
H | 0016491 | molecular_function | oxidoreductase activity |
H | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
H | 0019661 | biological_process | glucose catabolic process to lactate via pyruvate |
H | 0019752 | biological_process | carboxylic acid metabolic process |
H | 0035686 | cellular_component | sperm fibrous sheath |
H | 0042802 | molecular_function | identical protein binding |
H | 0042867 | biological_process | pyruvate catabolic process |
H | 0045296 | molecular_function | cadherin binding |
H | 0070062 | cellular_component | extracellular exosome |
H | 1990204 | cellular_component | oxidoreductase complex |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE NAI A 401 |
Chain | Residue |
A | GLY29 |
A | ALA98 |
A | ARG99 |
A | GLN100 |
A | PHE119 |
A | ILE120 |
A | VAL136 |
A | ASN138 |
A | SER161 |
A | HIS193 |
A | THR248 |
A | ALA30 |
A | ILE252 |
A | OXL402 |
A | HOH502 |
A | HOH540 |
A | HOH556 |
A | HOH561 |
A | HOH584 |
A | HOH585 |
G | ASN108 |
A | VAL31 |
A | ASP52 |
A | VAL53 |
A | ILE54 |
A | THR95 |
A | ALA96 |
A | GLY97 |
site_id | AC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE OXL A 402 |
Chain | Residue |
A | GLN100 |
A | ARG106 |
A | ASN138 |
A | ARG169 |
A | HIS193 |
A | ALA238 |
A | THR248 |
A | NAI401 |
A | HOH556 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 403 |
Chain | Residue |
A | ASN164 |
A | SER167 |
A | ARG171 |
A | PRO272 |
B | LEU70 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE OXL B 401 |
Chain | Residue |
B | ASN138 |
B | ARG169 |
B | HIS193 |
B | THR248 |
B | HOH592 |
site_id | AC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 B 402 |
Chain | Residue |
B | ARG171 |
B | HIS186 |
B | HOH516 |
B | HOH519 |
B | HOH541 |
B | HOH546 |
D | LEU183 |
D | HIS186 |
site_id | AC6 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE KAN B 403 |
Chain | Residue |
B | ASP52 |
B | VAL53 |
B | ALA96 |
B | GLY97 |
B | ARG99 |
B | ARG112 |
B | ILE116 |
B | PHE119 |
B | ILE120 |
H | GLU55 |
H | HOH556 |
site_id | AC7 |
Number of Residues | 30 |
Details | BINDING SITE FOR RESIDUE NAI C 401 |
Chain | Residue |
C | GLY29 |
C | ALA30 |
C | VAL31 |
C | ASP52 |
C | VAL53 |
C | ILE54 |
C | LYS57 |
C | THR95 |
C | ALA96 |
C | GLY97 |
C | ALA98 |
C | ARG99 |
C | ASN113 |
C | ILE120 |
C | VAL136 |
C | ASN138 |
C | SER161 |
C | HIS193 |
C | THR248 |
C | ILE252 |
C | OXL402 |
C | HOH503 |
C | HOH509 |
C | HOH525 |
C | HOH528 |
C | HOH544 |
C | HOH575 |
C | HOH579 |
C | HOH593 |
C | HOH604 |
site_id | AC8 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE OXL C 402 |
Chain | Residue |
C | LEU165 |
C | ARG169 |
C | HIS193 |
C | ALA238 |
C | THR248 |
C | NAI401 |
C | HOH544 |
C | GLN100 |
C | ARG106 |
C | ASN138 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 C 403 |
Chain | Residue |
C | ASN164 |
C | SER167 |
C | ARG171 |
C | PRO272 |
D | LEU70 |
site_id | BC1 |
Number of Residues | 34 |
Details | BINDING SITE FOR RESIDUE NAI D 401 |
Chain | Residue |
D | GLY29 |
D | ALA30 |
D | VAL31 |
D | ASP52 |
D | VAL53 |
D | ILE54 |
D | LYS57 |
D | THR95 |
D | ALA96 |
D | GLY97 |
D | ALA98 |
D | ARG99 |
D | GLN100 |
D | ASN113 |
D | ILE116 |
D | ILE120 |
D | VAL136 |
D | ASN138 |
D | SER161 |
D | LEU165 |
D | HIS193 |
D | THR248 |
D | ILE252 |
D | OXL402 |
D | HOH501 |
D | HOH525 |
D | HOH550 |
D | HOH563 |
D | HOH589 |
D | HOH590 |
D | HOH593 |
D | HOH629 |
E | GLY103 |
E | ASN108 |
site_id | BC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE OXL D 402 |
Chain | Residue |
D | GLN100 |
D | ARG106 |
D | ASN138 |
D | ARG169 |
D | HIS193 |
D | ALA238 |
D | THR248 |
D | NAI401 |
D | HOH589 |
site_id | BC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 D 403 |
Chain | Residue |
C | LEU70 |
D | ASN164 |
D | SER167 |
D | ARG171 |
D | PRO272 |
D | HOH596 |
site_id | BC4 |
Number of Residues | 30 |
Details | BINDING SITE FOR RESIDUE NAI E 401 |
Chain | Residue |
E | GLY29 |
E | ALA30 |
E | VAL31 |
E | ASP52 |
E | VAL53 |
E | ILE54 |
E | LYS57 |
E | THR95 |
E | ALA96 |
E | GLY97 |
E | ALA98 |
E | ARG99 |
E | GLN100 |
E | ASN113 |
E | ILE116 |
E | ILE120 |
E | VAL136 |
E | ASN138 |
E | SER161 |
E | LEU165 |
E | HIS193 |
E | THR248 |
E | ILE252 |
E | OXL402 |
E | HOH504 |
E | HOH509 |
E | HOH514 |
E | HOH547 |
E | HOH571 |
E | HOH575 |
site_id | BC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE OXL E 402 |
Chain | Residue |
E | GLN100 |
E | ARG106 |
E | ASN138 |
E | ARG169 |
E | HIS193 |
E | ALA238 |
E | THR248 |
E | NAI401 |
E | HOH514 |
site_id | BC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 E 403 |
Chain | Residue |
E | ASN164 |
E | SER167 |
E | ARG171 |
E | PRO272 |
site_id | BC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 E 404 |
Chain | Residue |
D | GLY97 |
D | ALA98 |
D | ILE116 |
D | HOH563 |
D | HOH578 |
E | ASN108 |
site_id | BC8 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE NAI F 401 |
Chain | Residue |
C | GLN111 |
F | GLY29 |
F | ALA30 |
F | VAL31 |
F | ASP52 |
F | VAL53 |
F | ILE54 |
F | LYS57 |
F | THR95 |
F | ALA96 |
F | GLY97 |
F | ALA98 |
F | ARG99 |
F | ILE116 |
F | VAL136 |
F | ASN138 |
F | SER161 |
F | HIS193 |
F | THR248 |
F | ILE252 |
F | OXL402 |
F | HOH501 |
F | HOH503 |
F | HOH544 |
F | HOH566 |
F | HOH567 |
F | HOH589 |
F | HOH596 |
site_id | BC9 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE OXL F 402 |
Chain | Residue |
F | GLN100 |
F | ARG106 |
F | ASN138 |
F | ARG169 |
F | HIS193 |
F | ALA238 |
F | THR248 |
F | NAI401 |
F | HOH596 |
site_id | CC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 F 403 |
Chain | Residue |
E | LEU70 |
F | ASN164 |
F | SER167 |
F | ARG171 |
F | PRO272 |
site_id | CC2 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE NAI G 401 |
Chain | Residue |
G | GLY29 |
G | ALA30 |
G | VAL31 |
G | ASP52 |
G | VAL53 |
G | ILE54 |
G | LYS57 |
G | THR95 |
G | ALA96 |
G | GLY97 |
G | ALA98 |
G | ARG99 |
G | GLN100 |
G | ILE116 |
G | VAL136 |
G | ASN138 |
G | SER161 |
G | LEU165 |
G | HIS193 |
G | THR248 |
G | ILE252 |
G | OXL402 |
G | HOH502 |
G | HOH510 |
G | HOH515 |
G | HOH530 |
G | HOH576 |
site_id | CC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE OXL G 402 |
Chain | Residue |
G | GLN100 |
G | ARG106 |
G | ASN138 |
G | ARG169 |
G | HIS193 |
G | ALA238 |
G | THR248 |
G | NAI401 |
site_id | CC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 G 403 |
Chain | Residue |
G | ASN164 |
G | SER167 |
G | ARG171 |
G | PRO272 |
H | LEU70 |
site_id | CC5 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE NAI H 401 |
Chain | Residue |
H | GLY29 |
H | ALA30 |
H | VAL31 |
H | ASP52 |
H | ILE54 |
H | THR95 |
H | ALA96 |
H | GLY97 |
H | ALA98 |
H | ARG99 |
H | ILE116 |
H | PHE119 |
H | ILE120 |
H | VAL136 |
H | ASN138 |
H | SER161 |
H | LEU165 |
H | HIS193 |
H | THR248 |
H | ILE252 |
H | OXL402 |
H | HOH502 |
H | HOH507 |
H | HOH517 |
H | HOH521 |
H | HOH550 |
site_id | CC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE OXL H 402 |
Chain | Residue |
H | GLN100 |
H | ARG106 |
H | ASN138 |
H | ARG169 |
H | HIS193 |
H | ALA238 |
H | THR248 |
H | NAI401 |
site_id | CC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 H 403 |
Chain | Residue |
G | LEU70 |
H | ASN164 |
H | SER167 |
H | ARG171 |
H | TRP188 |
H | PRO272 |
Functional Information from PROSITE/UniProt
site_id | PS00064 |
Number of Residues | 7 |
Details | L_LDH L-lactate dehydrogenase active site. LGEHGDS |
Chain | Residue | Details |
A | LEU190-SER196 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | Active site: {"description":"Proton acceptor"} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 232 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"11276087","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 32 |
Details | Binding site: {} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2005","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V."]}},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 24 |
Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P06151","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 8 |
Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 24 |
Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 8 |
Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 8 |
Details | Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 24 |
Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P06151","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI11 |
Number of Residues | 8 |
Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P06151","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI12 |
Number of Residues | 16 |
Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P04642","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI13 |
Number of Residues | 8 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI14 |
Number of Residues | 16 |
Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |