2XIJ

Crystal structure of human methylmalonyl-CoA mutase in complex with adenosylcobalamin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0003924	molecular_function	GTPase activity
A	0004494	molecular_function	methylmalonyl-CoA mutase activity
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005759	cellular_component	mitochondrial matrix
A	0006790	biological_process	sulfur compound metabolic process
A	0016853	molecular_function	isomerase activity
A	0016866	molecular_function	intramolecular transferase activity
A	0019678	biological_process	propionate metabolic process, methylmalonyl pathway
A	0031419	molecular_function	cobalamin binding
A	0042802	molecular_function	identical protein binding
A	0042803	molecular_function	protein homodimerization activity
A	0043547	biological_process	positive regulation of GTPase activity
A	0044281	biological_process	small molecule metabolic process
A	0046872	molecular_function	metal ion binding
A	0050667	biological_process	homocysteine metabolic process
A	0072341	molecular_function	modified amino acid binding
A	1901290	biological_process	succinyl-CoA biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	43
Details	BINDING SITE FOR RESIDUE B12 A 800

Chain	Residue
A	PHE138
A	GLU392
A	ALA393
A	LEU394
A	GLY395
A	GLN476
A	GLY626
A	HIS627
A	ASP628
A	ARG629
A	GLY630
A	LEU140
A	ILE634
A	GLY670
A	SER672
A	LEU674
A	ALA675
A	ALA676
A	GLY702
A	GLY703
A	VAL704
A	PHE722
A	HIS143
A	GLY723
A	PRO724
A	THR726
A	5AD1746
A	HOH2253
A	HOH2447
A	HOH2488
A	HOH2508
A	HOH3001
A	HOH3002
A	ALA160
A	HOH3003
A	HOH3004
A	HOH3005
A	HOH3006
A	VAL227
A	ARG228
A	THR230
A	GLU268
A	TRP356

---

site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE 5AD A 1746

Chain	Residue
A	ALA160
A	GLN352
A	LEU396
A	HOH2173
A	HOH2198
A	HOH2252
A	HOH2507
A	HOH2508
A	HOH2510
A	B12800

---

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 A 1747

Chain	Residue
A	ARG613
A	ARG613
A	ARG614
A	ARG614
A	ARG616
A	ARG616
A	HOH2511
A	HOH2511

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 1748

Chain	Residue
A	TYR146
A	ASN150
A	ARG152
A	HOH2512

---

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO A 1749

Chain	Residue
A	SER594
A	LYS595
A	GLU596
A	HOH2513

---

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A 1750

Chain	Residue
A	GLU65
A	ASP272
A	ILE274
A	HOH2035
A	HOH2514
A	HOH2515

---

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A 1751

Chain	Residue
A	ASP58
A	ILE60
A	TRP61
A	LYS420
A	HOH2030
A	HOH2516

---

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO A 1752

Chain	Residue
A	ARG108
A	SER306
A	HIS350
A	SER384

---

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A 1757

Chain	Residue
A	THR249
A	ALA250
A	SER258
A	ARG304
A	HOH2190
A	HOH2193

---

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 1753

Chain	Residue
A	GLU117
A	VAL510
A	GLN514
A	LYS517
A	HOH2517

---

site_id	BC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 1754

Chain	Residue
A	THR216
A	GLN218
A	SER260
A	PHE308
A	TYR110
A	SER185
A	MET186

---

site_id	BC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO A 1755

Chain	Residue
A	PRO695
A	ILE697
A	HOH2485

---

site_id	BC4
Number of Residues	11
Details	BINDING SITE FOR RESIDUE BTB A 1756

Chain	Residue
A	ILE107
A	ARG108
A	GLN109
A	TYR110
A	ALA111
A	GLN131
A	SER135
A	ARG406
A	HOH2079
A	HOH2520
A	HOH2521

---

Functional Information from PROSITE/UniProt

site_id	PS00544
Number of Residues	26
Details	METMALONYL_COA_MUTASE Methylmalonyl-CoA mutase signature. RIARNTqiIIqEEsgipKvaDPwGGS

Chain	Residue	Details
A	ARG403-SER428

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	15
Details	Binding site: {"evidences":[{"source":"PubMed","id":"20876572","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"20876572","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P16332","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P16332","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---